MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it http://mint.bio.uniroma2.it/mint anonymous-2014k-1 Structural and Energetic Basis of Isopropylmalate Dehydrogenase Enzyme Catalysis in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined manfred.weiss@helmholtz-berlin.de 2014 imex curation Palló A., Oláh J., Gráczer E., Merli A., Závodszky P., Weiss M.S., Vas M. FEBS J. (1742-464X) Only protein-protein interactions leu3_thet8 3-isopropylmalate dehydrogenase leuB 3-IPM-DH Beta-IPM dehydrogenase TTHA1230 protein protein thet8 Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) MKVAVLPGDGIGPEVTEAALKVLRALDEAEGLGLAYEVFPFGGAAIDAFGEPFPEPTRKGVEEAEAVLLGSVGGPKWDGLPRKIRPETGLLSLRKSQDLFANLRPAKVFPGLERLSPLKEEIARGVDVLIVRELTGGIYFGEPRGMSEAEAWNTERYSKPEVERVARVAFEAARKRRKHVVSVDKANVLEVGEFWRKTVEEVGRGYPDVALEHQYVDAMAMHLVRSPARFDVVVTGNIFGDILSDLASVLPGSLGLLPSASLGRGTPVFEPVHGSAPDIAGKGIANPTAAILSAAMMLEHAFGLVELARKVEDAVAKALLETPPPDLGGSAGTEAFTATVLRHLA leub-1 1567103 n/a Tt-IPMDH 1567104 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified his tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false Stoichiometry: 2.0 direct interaction direct interaction false false false t1 t2 f1 The four individual protein chains in the asymmetric unit of the crystal are very similar to each other with r.m.s. differences between the chains of about 0.2 Å, which is not significantly larger than the overall coordinate error of the structure. Each of the four chains harbors one NADH, one IPM, one Mn2+ and two K+ ions, one of them bound close to the active site. The chains A-D assemble into two functional dimers (AB and CD), which both exhibit a fully closed conformation, only slightly better closed than the previously published structure of the ternary complex Tt-IPMDH-Mn2+-IPM [17]. Overlaying of the various open, partially and fully closed forms are illustrated by Fig. 2A and 2B. The very same closed conformation was observed in a different crystal form (data not shown), which lends support to the biological relevance of this conformation.