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 Glutamate 270 plays an essential role in K(+)-activation and domain closure of Thermus thermophilus isopropylmalate dehydrogenase. Glutamate 270 plays an essential role in K(+)-activation and domain closure of Thermus thermophilus isopropylmalate dehydrogenase. FEBS Lett. (0014-5793) 2015 imex curation 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 Only protein-protein interactions 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 Accepted 2015-FEB-23 by LUANA 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 3EFF8736312E2785 leub-1 1 2 predetermined predetermined participant predetermined 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 E A Wed May 02 14:53:21 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu270ala' Tue Jun 30 19:18:23 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu270Ala' direct interaction direct interaction 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.