DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Structural and theoretical studies indicate that the cylindrical protease ClpP samples extended and compact conformations. Structural and theoretical studies indicate that the cylindrical protease ClpP samples extended and compact conformations. Structure (London, England : 1993) 2010 imex curation Kimber MS., Yu AY., Borg M., Leung E., Chan HS., Houry WA. Only protein-protein interactions ecolx Escherichia coli solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Kimber MS., Yu AY., Borg M., Leung E., Chan HS., Houry WA. DIP original experiment: DIP-217112X Structure (London, England : 1993) 2010 IMEx Structural and theoretical studies indicate that the cylindrical protease ClpP samples extended and compact conformations. Structural and theoretical studies indicate that the cylindrical protease ClpP samples extended and compact conformations. Structural and theoretical studies indicate that the cylindrical protease ClpP samples extended and compact conformations. Structure (London, England : 1993) 2010 imex curation Kimber MS., Yu AY., Borg M., Leung E., Chan HS., Houry WA. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Kimber MS., Yu AY., Borg M., Leung E., Chan HS., Houry WA. DIP original experiment: DIP-217108X Structure (London, England : 1993) 2010 IMEx Structural and theoretical studies indicate that the cylindrical protease ClpP samples extended and compact conformations. Structural and theoretical studies indicate that the cylindrical protease ClpP samples extended and compact conformations. Structural and theoretical studies indicate that the cylindrical protease ClpP samples extended and compact conformations. Structure (London, England : 1993) 2010 imex curation Kimber MS., Yu AY., Borg M., Leung E., Chan HS., Houry WA. Only protein-protein interactions ecolx Escherichia coli comigration in sds comigration in sds page comigration in sds predetermined predetermined participant predetermined Kimber MS., Yu AY., Borg M., Leung E., Chan HS., Houry WA. DIP original experiment: DIP-217111X Structure (London, England : 1993) 2010 IMEx Structural and theoretical studies indicate that the cylindrical protease ClpP samples extended and compact conformations. Structural and theoretical studies indicate that the cylindrical protease ClpP samples extended and compact conformations. Structural and theoretical studies indicate that the cylindrical protease ClpP samples extended and compact conformations. Structure (London, England : 1993) 2010 imex curation Kimber MS., Yu AY., Borg M., Leung E., Chan HS., Houry WA. 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 Kimber MS., Yu AY., Borg M., Leung E., Chan HS., Houry WA. DIP original experiment: DIP-217109X Structure (London, England : 1993) 2010 IMEx Structural and theoretical studies indicate that the cylindrical protease ClpP samples extended and compact conformations. Structural and theoretical studies indicate that the cylindrical protease ClpP samples extended and compact conformations. Structural and theoretical studies indicate that the cylindrical protease ClpP samples extended and compact conformations. Structure (London, England : 1993) 2010 imex curation Kimber MS., Yu AY., Borg M., Leung E., Chan HS., Houry WA. Only protein-protein interactions ecolx Escherichia coli solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Kimber MS., Yu AY., Borg M., Leung E., Chan HS., Houry WA. DIP original experiment: DIP-217110X Structure (London, England : 1993) 2010 IMEx Structural and theoretical studies indicate that the cylindrical protease ClpP samples extended and compact conformations. clpp_ecoli ATP-dependent Clp protease proteolytic subunit clpP lopP Endopeptidase Clp Caseinolytic protease Protease Ti Heat shock protein F21.5 b0437 JW0427 protein protein ecoli Escherichia coli (strain K12) MSYSGERDNFAPHMALVPMVIEQTSRGERSFDIYSRLLKERVIFLTGQVEDHMANLIVAQMLFLEAENPEKDIYLYINSPGGVITAGMSIYDTMQFIKPDVSTICMGQAASMGAFLLTAGAKGKRFCLPNSRVMIHQPLGGYQGQATDIEIHAREILKVKGRMNELMALHTGQSLEQIERDTERDRFLSAPEAVEYGLVDSILTHRN DIP protein P0A6G7 original sequence version: 51 DIP protein P0A6G7 original sequence version: 96 A7843D036C8CB3C2 clpp_human ATP-dependent Clp protease proteolytic subunit, mitochondrial CLPP Endopeptidase Clp protein protein human Homo sapiens Human MWPGILVGGARVASCRYPALGPRLAAHFPAQRPPQRTLQNGLALQRCLHATATRALPLIPIVVEQTGRGERAYDIYSRLLRERIVCVMGPIDDSVASLVIAQLLFLQSESNKKPIHMYINSPGGVVTAGLAIYDTMQYILNPICTWCVGQAASMGSLLLAAGTPGMRHSLPNSRIMIHQPSGGARGQATDIAIQAEEIMKLKKQLYNIYAKHTKQSLQVIESAMERDRYMSPMEAQEFGILDKVLVHPPQDGEDEPTLVQKEPVEAAPAAEPVPAST DIP protein Q16740 original sequence version: 95 B03AAC5D50F7880E clpp-6 2 6 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction clpp-7 1 7 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction clpp-8 4 6 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction clpp-9 5 6 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction clpp-10 3 6 unspecified role unspecified role unspecified role unspecified role A153C A153C binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli covalent binding covalent binding