DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations. Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations. Structure (London, England : 1993) 2013 imex curation Froese DS., Forouhar F., Tran TH., Vollmar M., Kim YS., Lew S., Neely H., Seetharaman J., Shen Y., Xiao R., Acton TB., Everett JK., Cannone G., Puranik S., Savitsky P., Krojer T., Pilka ES., Kiyani W., Lee WH., Marsden BD., von Delft F., Allerston CK., Spagnolo L., Gileadi O., Montelione GT., Oppermann U., Yue WW., Tong L. Only protein-protein interactions ecolx Escherichia coli light scattering light scattering predetermined predetermined participant predetermined Froese DS., Forouhar F., Tran TH., Vollmar M., Kim YS., Lew S., Neely H., Seetharaman J., Shen Y., Xiao R., Acton TB., Everett JK., Cannone G., Puranik S., Savitsky P., Krojer T., Pilka ES., Kiyani W., Lee WH., Marsden BD., von Delft F., Allerston CK., Spagnolo L., Gileadi O., Montelione GT., Oppermann U., Yue WW., Tong L. DIP original experiment: DIP-253983X Structure (London, England : 1993) 2013 IMEx Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations. Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations. Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations. Structure (London, England : 1993) 2013 imex curation Froese DS., Forouhar F., Tran TH., Vollmar M., Kim YS., Lew S., Neely H., Seetharaman J., Shen Y., Xiao R., Acton TB., Everett JK., Cannone G., Puranik S., Savitsky P., Krojer T., Pilka ES., Kiyani W., Lee WH., Marsden BD., von Delft F., Allerston CK., Spagnolo L., Gileadi O., Montelione GT., Oppermann U., Yue WW., Tong L. Only protein-protein interactions ecolx Escherichia coli solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Froese DS., Forouhar F., Tran TH., Vollmar M., Kim YS., Lew S., Neely H., Seetharaman J., Shen Y., Xiao R., Acton TB., Everett JK., Cannone G., Puranik S., Savitsky P., Krojer T., Pilka ES., Kiyani W., Lee WH., Marsden BD., von Delft F., Allerston CK., Spagnolo L., Gileadi O., Montelione GT., Oppermann U., Yue WW., Tong L. DIP original experiment: DIP-253974X Structure (London, England : 1993) 2013 IMEx Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations. Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations. Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations. Structure (London, England : 1993) 2013 imex curation Froese DS., Forouhar F., Tran TH., Vollmar M., Kim YS., Lew S., Neely H., Seetharaman J., Shen Y., Xiao R., Acton TB., Everett JK., Cannone G., Puranik S., Savitsky P., Krojer T., Pilka ES., Kiyani W., Lee WH., Marsden BD., von Delft F., Allerston CK., Spagnolo L., Gileadi O., Montelione GT., Oppermann U., Yue WW., Tong L. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Froese DS., Forouhar F., Tran TH., Vollmar M., Kim YS., Lew S., Neely H., Seetharaman J., Shen Y., Xiao R., Acton TB., Everett JK., Cannone G., Puranik S., Savitsky P., Krojer T., Pilka ES., Kiyani W., Lee WH., Marsden BD., von Delft F., Allerston CK., Spagnolo L., Gileadi O., Montelione GT., Oppermann U., Yue WW., Tong L. DIP original experiment: DIP-253976X Structure (London, England : 1993) 2013 IMEx Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations. Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations. Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations. Structure (London, England : 1993) 2013 imex curation Froese DS., Forouhar F., Tran TH., Vollmar M., Kim YS., Lew S., Neely H., Seetharaman J., Shen Y., Xiao R., Acton TB., Everett JK., Cannone G., Puranik S., Savitsky P., Krojer T., Pilka ES., Kiyani W., Lee WH., Marsden BD., von Delft F., Allerston CK., Spagnolo L., Gileadi O., Montelione GT., Oppermann U., Yue WW., Tong L. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Froese DS., Forouhar F., Tran TH., Vollmar M., Kim YS., Lew S., Neely H., Seetharaman J., Shen Y., Xiao R., Acton TB., Everett JK., Cannone G., Puranik S., Savitsky P., Krojer T., Pilka ES., Kiyani W., Lee WH., Marsden BD., von Delft F., Allerston CK., Spagnolo L., Gileadi O., Montelione GT., Oppermann U., Yue WW., Tong L. DIP original experiment: DIP-253979X Structure (London, England : 1993) 2013 IMEx Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations. Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations. Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations. Structure (London, England : 1993) 2013 imex curation Froese DS., Forouhar F., Tran TH., Vollmar M., Kim YS., Lew S., Neely H., Seetharaman J., Shen Y., Xiao R., Acton TB., Everett JK., Cannone G., Puranik S., Savitsky P., Krojer T., Pilka ES., Kiyani W., Lee WH., Marsden BD., von Delft F., Allerston CK., Spagnolo L., Gileadi O., Montelione GT., Oppermann U., Yue WW., Tong L. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Froese DS., Forouhar F., Tran TH., Vollmar M., Kim YS., Lew S., Neely H., Seetharaman J., Shen Y., Xiao R., Acton TB., Everett JK., Cannone G., Puranik S., Savitsky P., Krojer T., Pilka ES., Kiyani W., Lee WH., Marsden BD., von Delft F., Allerston CK., Spagnolo L., Gileadi O., Montelione GT., Oppermann U., Yue WW., Tong L. DIP original experiment: DIP-253977X Structure (London, England : 1993) 2013 IMEx Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations. Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations. Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations. Structure (London, England : 1993) 2013 imex curation Froese DS., Forouhar F., Tran TH., Vollmar M., Kim YS., Lew S., Neely H., Seetharaman J., Shen Y., Xiao R., Acton TB., Everett JK., Cannone G., Puranik S., Savitsky P., Krojer T., Pilka ES., Kiyani W., Lee WH., Marsden BD., von Delft F., Allerston CK., Spagnolo L., Gileadi O., Montelione GT., Oppermann U., Yue WW., Tong L. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Froese DS., Forouhar F., Tran TH., Vollmar M., Kim YS., Lew S., Neely H., Seetharaman J., Shen Y., Xiao R., Acton TB., Everett JK., Cannone G., Puranik S., Savitsky P., Krojer T., Pilka ES., Kiyani W., Lee WH., Marsden BD., von Delft F., Allerston CK., Spagnolo L., Gileadi O., Montelione GT., Oppermann U., Yue WW., Tong L. DIP original experiment: DIP-253982X Structure (London, England : 1993) 2013 IMEx Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations. Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations. Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations. Structure (London, England : 1993) 2013 imex curation Froese DS., Forouhar F., Tran TH., Vollmar M., Kim YS., Lew S., Neely H., Seetharaman J., Shen Y., Xiao R., Acton TB., Everett JK., Cannone G., Puranik S., Savitsky P., Krojer T., Pilka ES., Kiyani W., Lee WH., Marsden BD., von Delft F., Allerston CK., Spagnolo L., Gileadi O., Montelione GT., Oppermann U., Yue WW., Tong L. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Froese DS., Forouhar F., Tran TH., Vollmar M., Kim YS., Lew S., Neely H., Seetharaman J., Shen Y., Xiao R., Acton TB., Everett JK., Cannone G., Puranik S., Savitsky P., Krojer T., Pilka ES., Kiyani W., Lee WH., Marsden BD., von Delft F., Allerston CK., Spagnolo L., Gileadi O., Montelione GT., Oppermann U., Yue WW., Tong L. DIP original experiment: DIP-253978X Structure (London, England : 1993) 2013 IMEx Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations. Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations. Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations. Structure (London, England : 1993) 2013 imex curation Froese DS., Forouhar F., Tran TH., Vollmar M., Kim YS., Lew S., Neely H., Seetharaman J., Shen Y., Xiao R., Acton TB., Everett JK., Cannone G., Puranik S., Savitsky P., Krojer T., Pilka ES., Kiyani W., Lee WH., Marsden BD., von Delft F., Allerston CK., Spagnolo L., Gileadi O., Montelione GT., Oppermann U., Yue WW., Tong L. Only protein-protein interactions ecolx Escherichia coli tem transmission electron microscopy tem predetermined predetermined participant predetermined Froese DS., Forouhar F., Tran TH., Vollmar M., Kim YS., Lew S., Neely H., Seetharaman J., Shen Y., Xiao R., Acton TB., Everett JK., Cannone G., Puranik S., Savitsky P., Krojer T., Pilka ES., Kiyani W., Lee WH., Marsden BD., von Delft F., Allerston CK., Spagnolo L., Gileadi O., Montelione GT., Oppermann U., Yue WW., Tong L. DIP original experiment: DIP-253975X Structure (London, England : 1993) 2013 IMEx Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations. Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations. Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations. Structure (London, England : 1993) 2013 imex curation Froese DS., Forouhar F., Tran TH., Vollmar M., Kim YS., Lew S., Neely H., Seetharaman J., Shen Y., Xiao R., Acton TB., Everett JK., Cannone G., Puranik S., Savitsky P., Krojer T., Pilka ES., Kiyani W., Lee WH., Marsden BD., von Delft F., Allerston CK., Spagnolo L., Gileadi O., Montelione GT., Oppermann U., Yue WW., Tong L. Only protein-protein interactions ecolx Escherichia coli light scattering light scattering predetermined predetermined participant predetermined Froese DS., Forouhar F., Tran TH., Vollmar M., Kim YS., Lew S., Neely H., Seetharaman J., Shen Y., Xiao R., Acton TB., Everett JK., Cannone G., Puranik S., Savitsky P., Krojer T., Pilka ES., Kiyani W., Lee WH., Marsden BD., von Delft F., Allerston CK., Spagnolo L., Gileadi O., Montelione GT., Oppermann U., Yue WW., Tong L. DIP original experiment: DIP-253981X Structure (London, England : 1993) 2013 IMEx Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations. Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations. Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations. Structure (London, England : 1993) 2013 imex curation Froese DS., Forouhar F., Tran TH., Vollmar M., Kim YS., Lew S., Neely H., Seetharaman J., Shen Y., Xiao R., Acton TB., Everett JK., Cannone G., Puranik S., Savitsky P., Krojer T., Pilka ES., Kiyani W., Lee WH., Marsden BD., von Delft F., Allerston CK., Spagnolo L., Gileadi O., Montelione GT., Oppermann U., Yue WW., Tong L. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Froese DS., Forouhar F., Tran TH., Vollmar M., Kim YS., Lew S., Neely H., Seetharaman J., Shen Y., Xiao R., Acton TB., Everett JK., Cannone G., Puranik S., Savitsky P., Krojer T., Pilka ES., Kiyani W., Lee WH., Marsden BD., von Delft F., Allerston CK., Spagnolo L., Gileadi O., Montelione GT., Oppermann U., Yue WW., Tong L. DIP original experiment: DIP-253980X Structure (London, England : 1993) 2013 IMEx Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations. Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations. Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations. Structure (London, England : 1993) 2013 imex curation Froese DS., Forouhar F., Tran TH., Vollmar M., Kim YS., Lew S., Neely H., Seetharaman J., Shen Y., Xiao R., Acton TB., Everett JK., Cannone G., Puranik S., Savitsky P., Krojer T., Pilka ES., Kiyani W., Lee WH., Marsden BD., von Delft F., Allerston CK., Spagnolo L., Gileadi O., Montelione GT., Oppermann U., Yue WW., Tong L. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Froese DS., Forouhar F., Tran TH., Vollmar M., Kim YS., Lew S., Neely H., Seetharaman J., Shen Y., Xiao R., Acton TB., Everett JK., Cannone G., Puranik S., Savitsky P., Krojer T., Pilka ES., Kiyani W., Lee WH., Marsden BD., von Delft F., Allerston CK., Spagnolo L., Gileadi O., Montelione GT., Oppermann U., Yue WW., Tong L. DIP original experiment: DIP-253973X Structure (London, England : 1993) 2013 IMEx Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations. q1ljk6_cupmc matA Rmet_2797 protein protein cupmc Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34) Ralstonia metallidurans MTALDTSDQQKVSAPLDAAEPVSDTLLSRFGRWWNRKGDADATAAGPAKAQDTPALSTRATKRQRDQLRQCFDARLTDVAANAAAQAWQDEYEAAVEPLRQAMLGVLAEVAAVRDAAGGQPATASGLSQALSNARIRFFKRFAALHGQRGNSACGLHFLIQLRADMLRWHKRIPGLRELDEDLEALFSNWFDVGLLELQPITWDSPASLLEKLIRYEAVHEISSWTDLRNRLDSDRRCYAFFHPRIPREPLIFVEVAFVPEMAANVQALLDEAAPLEDLRRVKWAIFYSISNTQAGLRGVSFGNFLLKRVIEELQREHPKLKQFATLSPIPGFADWLRKRDGESIDRVLGVKRLARWREQHGEVPADGAAWFSALSADTEDTVIRDTAMTLAAHYLVREGGKGVPADPVARFHLGNGACVERVNWGADMSRKGRAQSCGMMVNYLYVPDALDDNLARLGDGNPRISRAVAKLL DIP protein Q1LJK6 original sequence version: 39 dcmc_human Malonyl-CoA decarboxylase, mitochondrial MLYCD protein protein human Homo sapiens Human MRGFGPGLTARRLLPLRLPPRPPGPRLASGQAAGALERAMDELLRRAVPPTPAYELREKTPAPAEGQCADFVSFYGGLAETAQRAELLGRLARGFGVDHGQVAEQSAGVLHLRQQQREAAVLLQAEDRLRYALVPRYRGLFHHISKLDGGVRFLVQLRADLLEAQALKLVEGPDVREMNGVLKGMLSEWFSSGFLNLERVTWHSPCEVLQKISEAEAVHPVKNWMDMKRRVGPYRRCYFFSHCSTPGEPLVVLHVALTGDISSNIQAIVKEHPPSETEEKNKITAAIFYSISLTQQGLQGVELGTFLIKRVVKELQREFPHLGVFSSLSPIPGFTKWLLGLLNSQTKEHGRNELFTDSECKEISEITGGPINETLKLLLSSSEWVQSEKLVRALQTPLMRLCAWYLYGEKHRGYALNPVANFHLQNGAVLWRINWMADVSLRGITGSCGLMANYRYFLEETGPNSTSYLGSKIIKASEQVLSLVAQFQKNSKL DIP protein O95822 original sequence version: 116 8F061CA38908E8FC b9k0v9_agrvs Avi_5372 protein protein agrvs Agrobacterium vitis (strain S4 / ATCC BAA-846) Rhizobium vitis (strain S4) MAGTSFLSDLLSGVTERGRALLFSGSKARDRVVDTDIETLCEMLLSSRGEASGMAIAAEILDRWSRFNAAEAVQFLHMLSDRFGAEAAALDKAIDAYRTDKSPMAVIALHNAAEPRRQELLRRLNLAPNGTQKLVRMRERLLETKEDRADLGAVDTDFAHLFSSWFNRGFLTLQPIDWTTPAHILEKIIKYEAVHEIAGWEELRRRLAPADRRCFAFFHPRLRDDPLVFVEVALTRSIPSAIADVLDESRDHIGADTATTAVFYSISNCQDGLRGISFGNFLIKQVVEDLRRDLPGLKEFVTLSPVPGFARWISKIRDPKSGFPLSPEDRNTLVLLDDPTWPEDKARADAVERILLPLAARYFITERTPDNRPVDPVARFHLGNGARLERLNFLGDRSVKAMRQAHGLMVNYLYKLEDIETNHEALAQRGEVAASPAVKALQGKIEPILPEKPKDIKKAESLSGS DIP protein B9K0V9 original sequence version: 24 q6ncb2_rhopa MCD MLYCD RPA0560 protein protein rhopa Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) MKLMPIATTADRASEFLGGLFNSLTERGRSLFGLTSSQPMSGDELIALSETLLSRRGEASGVALAASLLAGYEAADEDDKLAFLDALAEQFGPDLAELNTAIEAFRADASAEATGELLRAAEPRRQELIRRLNHAPGGTAALVKMREAVLARIAAHPQLRHVDDDFVHLFTSWFNRGFLVLQRIDWTTPANILEKIIRYEQVHTIHDWDDLRARLAPPDRRCYGFFHPRLVDEPLIFVEVALTKDSPAAIAPLLDLEREPIAASDATTAVFYSISNTQQGLAGISFGNFLIKQVVEEIKRELPNVQTFVTLSPVPGFAKWLKRERDNPDSTLLDASARTALEALDTPNWFDDADTADRLKPIVLQLAAAYFLQAKGPNGRPLDPVARFHLGNGARLDRLNFLGDRSPNGMRQSHGLMVNYLYALGDIEANHEALFERGQIAAASAVRKLVPTKPVTSEPRKGNGKTASAPQAAPTA DIP protein Q6NCB2 original sequence version: 41 b9k0v9_agrvs-1 1 14 unspecified role unspecified role unspecified role unspecified role Region 1-448 Region 1-448 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction mlycd-1 11 13 unspecified role unspecified role unspecified role unspecified role Region 40-491 Region 40-491 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction mlycd-2 3 13 unspecified role unspecified role unspecified role unspecified role Region 40-491 Region 40-491 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction mcd-1 5 15 unspecified role unspecified role unspecified role unspecified role Region 8-451 Region 8-451 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction mlycd-3 2 13 unspecified role unspecified role unspecified role unspecified role Region 40-491 Region 40-491 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction mcd-2 10 15 unspecified role unspecified role unspecified role unspecified role Region 8-451 Region 8-451 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction mlycd-4 8 13 unspecified role unspecified role unspecified role unspecified role Region 40-491 Region 40-491 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction b9k0v9_agrvs-2 7 14 unspecified role unspecified role unspecified role unspecified role Region 1-448 Region 1-448 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction mcd-3 9 15 unspecified role unspecified role unspecified role unspecified role Region 8-451 Region 8-451 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction b9k0v9_agrvs-3 6 14 unspecified role unspecified role unspecified role unspecified role Region 1-448 Region 1-448 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction mata-1 4 12 unspecified role unspecified role unspecified role unspecified role Region 57-473 Region 57-473 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction