5ER6
Crystal structure of an oxidoreductase from Brucella ovis
Summary for 5ER6
| Entry DOI | 10.2210/pdb5er6/pdb |
| Descriptor | Oxidoreductase, short chain dehydrogenase/reductase family, ACETATE ION, 1,2-ETHANEDIOL, ... (4 entities in total) |
| Functional Keywords | ssgcid, oxidoreductase, short chain dehydrogenase/reductase family, brucella ovis, structural genomics, seattle structural genomics center for infectious disease |
| Biological source | Brucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512) |
| Total number of polymer chains | 4 |
| Total formula weight | 103863.10 |
| Authors | Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2015-11-13, release date: 2015-11-25, Last modification date: 2025-12-10) |
| Primary citation | Zupko, S.P.,Konstanty, A.T.,Mayclin, S.J.,Choi, R.,Serbzhinskiy, D.,Robles, E.,Moses, V.,Barrett, L.K.,Van Voorhis, W.C.,Edwards, T.E.,Myler, P.J.,Torelli, A.T.,French, J.B.,Hicks, K.A. Crystal structure of a short-chain dehydrogenase from Brucella ovis with apo and coenzyme NAD + -bound protomer chains. Acta Crystallogr.,Sect.F, 2025 Cited by PubMed Abstract: Short-chain dehydrogenases (SDRs) are a family of NAD(P)-dependent enzymes involved in redox reactions, specifically carbonyl-alcohol reductions. Here, we report the apo and NAD-bound structures of an SDR from the pathogenic organism Brucella ovis. B. ovis primarily affects sheep and other livestock, resulting in reduced fertility. Based on sequence and structural alignment, the B. ovis SDR (BoSDR) is a classical SDR. Classical SDRs have a canonical YxxxK active-site sequence in which the catalytic general base is a tyrosine residue located at position 163. In addition, the putative active site also contains a serine residue (Ser150) and lysine residue (Lys167) that are hypothesized to be involved in catalysis. BoSDR is a biological and crystallographic tetramer. In the coenzyme-bound structure, two different orientations of the NAD coenzyme are fortuitously observed, which provides insights into the conformational changes that accompany coenzyme binding. The apo and NAD-bound structures provide valuable information about the unique structural features of enzymes in the SDR superfamily. PubMed: 41216818DOI: 10.1107/S2053230X25009227 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.55 Å) |
Structure validation
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