Shah Bhumika S, Tetu Sasha G, Harrop Stephen J, Paulsen Ian T, Mabbutt Bridget C
Department of Chemistry and Biomolecular Sciences, Macquarie University, Research Park Drive, Sydney, NSW 2109, Australia.
School of Physics, University of New South Wales, Sydney, NSW 2052, Australia.
Acta Crystallogr F Struct Biol Commun. 2014 Oct;70(Pt 10):1318-23. doi: 10.1107/S2053230X14019785. Epub 2014 Sep 25.
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.
一株澳大利亚鲍曼不动杆菌临床分离株基因组中超过15%的部分存在于基因组岛中。对该菌株以及其他国际克隆II菌株共有的一个岛状特征区域内编码的一种未鉴定蛋白质进行了X射线晶体学研究。SDR-WM99c的2.4 Å分辨率结构显示它是经典短链脱氢酶/还原酶（SDR）超家族的一个新成员。该酶含有一个核苷酸结合结构域，并且与许多其他SDR一样，呈四聚体形式。活性位点包含一个催化四联体（Asn117、Ser146、Tyr159和Lys163）以及占据假定的NADP辅因子结合口袋的水分子。一个相邻的裂隙由一个相对可移动的螺旋亚结构域覆盖，该亚结构域位置恰当，可控制底物进入。
