3VMJ
3-isopropylmalate dehydrogenase from Shewanella oneidensis MR-1
Summary for 3VMJ
| Entry DOI | 10.2210/pdb3vmj/pdb |
| Related | 3VMK 3VML |
| Descriptor | 3-isopropylmalate dehydrogenase, 3-ISOPROPYLMALIC ACID, MAGNESIUM ION, ... (5 entities in total) |
| Functional Keywords | oxidoreductase, decarboxylating dehydrogenase |
| Biological source | Shewanella oneidensis |
| Cellular location | Cytoplasm : Q8E9N3 |
| Total number of polymer chains | 1 |
| Total formula weight | 40925.23 |
| Authors | Nagae, T.,Watanabe, N. (deposition date: 2011-12-13, release date: 2012-02-29, Last modification date: 2023-11-08) |
| Primary citation | Nagae, T.,Kato, C.,Watanabe, N. Structural analysis of 3-isopropylmalate dehydrogenase from the obligate piezophile Shewanella benthica DB21MT-2 and the nonpiezophile Shewanella oneidensis MR-1 Acta Crystallogr.,Sect.F, 68:265-268, 2012 Cited by PubMed Abstract: Organisms living in deep seas such as the Mariana Trench must be adapted to the extremely high pressure environment. For example, the 3-isopropylmalate dehydrogenase from the obligate piezophile Shewanella benthica DB21MT-2 (SbIPMDH) remains active in extreme conditions under which that from the land bacterium S. oneidensis MR-1 (SoIPMDH) becomes inactivated. In order to unravel the differences between these two IPMDHs, their structures were determined at ~1.5 Å resolution. Comparison of the structures of the two enzymes shows that SbIPMDH is in a more open form and has a larger internal cavity volume than SoIPMDH at atmospheric pressure. This loosely packed structure of SbIPMDH could help it to avoid pressure-induced distortion of the native structure and to remain active at higher pressures than SoIPMDH. PubMed: 22442218DOI: 10.1107/S1744309112001443 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.56 Å) |
Structure validation
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