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首页> 外文期刊>Journal of Molecular Biology >The structural basis of riboflavin binding to Schizosaccharomyces pombe 6,7-dimethyl-8-ribityllumazine synthase.
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The structural basis of riboflavin binding to Schizosaccharomyces pombe 6,7-dimethyl-8-ribityllumazine synthase.

机译：核黄素与粟酒裂殖酵母6,7-二甲基-8-核黄素合酶结合的结构基础。

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摘要

Riboflavin is an essential cofactor in all organisms. Its direct biosynthetic precursor, 6,7-dimethyl-8-ribityllumazine, is synthesised by the enzyme 6,7-dimethyl-8-ribityllumazine synthase. Recently, we have found that the enzyme from Schizosaccharomyces pombe binds riboflavin, the final product of the pathway with a relatively high affinity with a KD of 1.2 microM. Here, we report on the crystal structure of lumazine synthase from S. pombe with bound riboflavin and compare the binding mode with those of the substrate analogue inhibitor 5-nitro-6-(D-ribitylamino)-2,4(1H,3H)-pyrimidinedione and of the product analogue 6-carboxyethyl-7-oxo-8-ribityllumazine. In all complexes the pyrimidinedione moieties of each respective ligand bind in a very similar orientation. Binding of riboflavin additionally involves a stacking interaction of the dimethylbenzene moiety with the side-chain of His94, a highly conserved residue in all lumazine synthases. The enzyme from Bacillus subtilis showed a KD of at least 1 mM whereas the very homologous enzyme from Saccharomyces cerevisiae had a comparable KD of 3.9 microM. Structural comparison of the S. cerevisiae, the S. pombe, and the mutant enzymes suggests that fine tuning of affinity is achieved by influencing this stacking interaction.
机译：核黄素是所有生物中必不可少的辅助因子。它的直接生物合成前体6,7-二甲基-8-ribityllumazine由酶6,7-二甲基-8-ribityllumazine合酶合成。最近，我们发现来自粟酒裂殖酵母的酶与核黄素结合，核黄素是该途径的最终产物，与KD为1.2 microM具有相对较高的亲和力。在这里，我们报告与结合的核黄素的粟酒裂殖酵母的lumazine合酶的晶体结构，并与底物类似物抑制剂5-nitro-6-（D-ribitylamino）-2,4（1H，3H）的结合方式进行比较。 -嘧啶二酮及其产物类似物6-羧乙基-7-氧代-8-ribityllumazine。在所有复合物中，每个各自的配体的嘧啶二酮部分以非常相似的取向结合。核黄素的结合还涉及二甲基苯部分与His94侧链的堆积相互作用，His94是所有lumazine合成酶中高度保守的残基。来自枯草芽孢杆菌的酶显示至少1 mM的KD，而来自酿酒酵母的非常同源的酶具有3.9 microM的可比KD。酿酒酵母，粟酒裂殖酵母和突变酶的结构比较表明，亲和力的微调是通过影响这种堆积相互作用来实现的。

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