Structure of zinc-independent sorbitol dehydrogenase from Rhodobacter sphaeroides at 2.4 angstrom resolution

Philippsen A; Schirmer T; Stein MAGiffhorn FStetefeld J

首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structure of zinc-independent sorbitol dehydrogenase from Rhodobacter sphaeroides at 2.4 angstrom resolution

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Structure of zinc-independent sorbitol dehydrogenase from Rhodobacter sphaeroides at 2.4 angstrom resolution

机译：结构zinc-independent山梨糖醇脱氢酶从Rhodobacter sphaeroides为2.4埃分辨率

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Recombinant sorbitol dehydrogenase (SDH) from Rhodobacter sphaeroides has been crystallized in the absence of the cofactor NAD(H) and its structure determined to 2.4 angstrom resolution using molecular replacement (refined R and R-free factors of 18.8 and 23.8%, respectively). As expected from the sequence and shown by the conserved fold, SDH can be assigned to the short-chain dehydrogenase/reductase protein family. The cofactor NAD and the substrate sorbitol have been modelled into the structure and the active-site architecture, which displays the highly conserved catalytic tetrad of Asn-Ser-Tyr-Lys residues, is discussed in relation to the enzyme mechanism. This is the first structure of a bacterial SDH belonging to the SDR family.

机译：重组山梨糖醇脱氢酶(SDH)Rhodobacter sphaeroides一直在结晶代数余子式的缺席NAD (H)和它的结构决定2.4埃分辨率使用分子置换(精制R和有空因素分别为23.8%和18.8)。从序列和所表现出的预期守恒的褶皱,SDH可以分配给短链脱氢酶/还原酶蛋白质家庭。山梨糖醇被模仿到结构和活性部位的架构,它显示的高度保守的催化四分体Asn-Ser-Tyr-Lys残留物,讨论了与酶的机制。第一个细菌SDH属于结构特别提款权的家庭。

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《Acta crystallographica.Section D. Biological crystallography》 |2005年第4期|374-379|共6页
作者
Philippsen A; Schirmer T; Stein MAGiffhorn FStetefeld J;
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作者单位

Univ Basel, Biozentrum, Div Struct Biol, CH-4056 Basel, Switzerland;

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正文语种英语
中图分类化学;
关键词
enzyme mechanism; L-Iditol 2-Dehydrogenase; Rhodobacter sphaeroidesAngstrom;

机译：酶机制;L-Iditol2-Dehydrogenase;Rhodobacter sphaeroidesAngstrom;

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Structure of zinc-independent sorbitol dehydrogenase from Rhodobacter sphaeroides at 2.4 angstrom resolution

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