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 gr_czer-2015-1 Glutamate 270 plays an essential role in K(+)-activation and domain closure of Thermus thermophilus isopropylmalate dehydrogenase. in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Gráczer É., Palló A., Oláh J., Szimler T., Konarev P.V., Svergun D.I., Merli A., Závodszky P., Weiss M.S., Vas M. vas.maria@ttk.mta.hu FEBS Lett. (0014-5793) 2015 Only protein-protein interactions imex curation 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 1779379 n/a 1779380 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Q5SIY4:p.Glu270Ala mutation mutation certain certain sequence position certain certain certain sequence position certain false Stoichiometry: 2.0 direct interaction direct interaction false false false t1 f1 The global structure of E270A mutant IPMDH with bound Mn2+, IPM and NADH exhibits a closed conformation, but slightly less closed than that of the previously determined [7] wild-type enzyme. However, the active sites exhibit well defined differences due to the mutation. Fig. 1 illustrates part of the active site of Tt-IPMDH with bound IPM and NADH both of the wild-type (A) and the E270A mutant (B) enzymes. In the wild-type enzyme the carboxylate group of E270 is an important electrostatic ligand for K+-ion. In the active site of the wild-type IPMDH there was a peak observed on the Fo Fc difference density map when the K+-ion was initially modelled as water, however in case of the E270A mutant enzyme there was no residual density when this peak was modelled as water.