4IUY
Crystal structure of short-chain dehydrogenase/reductase (apo-form) from A. baumannii clinical strain WM99C
4IUY の概要
| エントリーDOI | 10.2210/pdb4iuy/pdb |
| 分子名称 | Short chain dehydrogenase/reductase (2 entities in total) |
| 機能のキーワード | rossmann fold, oxidoreductase |
| 由来する生物種 | Acinetobacter baumannii |
| タンパク質・核酸の鎖数 | 8 |
| 化学式量合計 | 242788.51 |
| 構造登録者 | Shah, B.S.,Tetu, S.G.,Harrop, S.J.,Paulsen, I.T.,Mabbutt, B.C. (登録日: 2013-01-21, 公開日: 2013-03-06, 最終更新日: 2024-11-20) |
| 主引用文献 | Shah, B.S.,Tetu, S.G.,Harrop, S.J.,Paulsen, I.T.,Mabbutt, B.C. Structure of a short-chain dehydrogenase/reductase (SDR) within a genomic island from a clinical strain of Acinetobacter baumannii. Acta Crystallogr.,Sect.F, 70:1318-1323, 2014 Cited by PubMed Abstract: Over 15% of the genome of an Australian clinical isolate of Acinetobacter baumannii occurs within genomic islands. An uncharacterized protein encoded within one island feature common to this and other International Clone II strains has been studied by X-ray crystallography. The 2.4 Å resolution structure of SDR-WM99c reveals it to be a new member of the classical short-chain dehydrogenase/reductase (SDR) superfamily. The enzyme contains a nucleotide-binding domain and, like many other SDRs, is tetrameric in form. The active site contains a catalytic tetrad (Asn117, Ser146, Tyr159 and Lys163) and water molecules occupying the presumed NADP cofactor-binding pocket. An adjacent cleft is capped by a relatively mobile helical subdomain, which is well positioned to control substrate access. PubMed: 25286932DOI: 10.1107/S2053230X14019785 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.385 Å) |
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