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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Active-site models for complexes of quinolinate synthase with substrates and intermediates
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Active-site models for complexes of quinolinate synthase with substrates and intermediates

机译:quinolinate复合物的活性位点模型合酶底物和中间体

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摘要

Quinolinate synthase (QS) catalyzes the condensation of iminoaspartate and dihydroxyacetone phosphate to form quinolinate, the universal precursor for the de novo biosynthesis of nicotinamide adenine dinucleotide. QS has been difficult to characterize owing either to instability or lack of activity when it is overexpressed and purified. Here, the structure of QS from Pyrococcus furiosus has been determined at 2.8? resolution. The structure is a homodimer consisting of three domains per protomer. Each domain shows the same topology with a four-stranded parallel β-sheet flanked by four -helices, suggesting that the domains are the result of gene triplication. Biochemical studies of QS indicate that the enzyme requires a [4Fe-4S] cluster, which is lacking in this crystal structure, for full activity. The organization of domains in the protomer is distinctly different from that of a monomeric structure of QS from P. horikoshii [Sakuraba et al. (2005), J. Biol. Chem. 280, 26645-26648]. The domain arrangement in P. furiosus QS may be related to protection of cysteine side chains, which are required to chelate the [4Fe-4S] cluster, prior to cluster assembly.
机译:Quinolinate合成酶(QS)催化iminoaspartate凝结,二羟丙酮磷酸形成quinolinate,新创的普遍的前兆烟酰胺腺嘌呤生物合成的二核苷酸。描述由于不稳定或缺乏时的活动中净化。海床furiosus已经确定在2.8吗?决议。每个原体组成的三个领域。域显示相同的拓扑结构四股平行β片两侧是四个螺旋,这表明域由于基因的三倍。QS表明酶的需要[4 fe-4s]集群,这是缺乏这一点晶体结构,完整的活动。域的组织原体从一个单体的截然不同结构的QS p horikoshii [Sakuraba等艾尔。(2005),生物。域在p . furiosus QS可能安排有关保护半胱氨酸的侧链,这需要螯合[4 fe-4s]集群,集群之前组装。

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