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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Crystal structure of glutamate-1-semialdehyde aminomutase: An α _2-dimeric vitamin B_6-dependent enzyme with asymmetry in structure and active site reactivity
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Crystal structure of glutamate-1-semialdehyde aminomutase: An α _2-dimeric vitamin B_6-dependent enzyme with asymmetry in structure and active site reactivity

机译:谷氨酸-1-半醛氨基变位酶的晶体结构:α_2-二聚体维生素B_6依赖性酶,结构和活性位点反应性均不对称

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摘要

The three-dimensional structure of gluta- mate-1-semialdehyde aminomutase (EC 5.4.3.8), an α_2- dimeric enzyme from Synechococcus, has been determined by x-ray crystallography using heavy atom derivative phasing. The structure, refined at 2.4-A deg resolution to an R-factor of 18.7/100 and good stereochemistry, explains many of the en- zyme's unusual specificity and functional properties. The overall fold is that of aspartate aminotransferase and related B6 enzymes, but it also has specific features. The structure of the complex with gabaculine, a substrate analogue, shows unexpectedly that the substrate binding site involves residues from the N-terminal domain of the molecule, notably Arg-32.
机译:谷氨酸-1-半醛氨基变位酶(EC 5.4.3.8)的三维结构(Synechococcus的一种α_2-二聚酶)已通过X射线晶体学使用重原子衍生物定相法确定。该结构以2.4A deg的分辨率精炼到18.7 / 100的R因子和良好的立体化学,解释了许多酶的不同寻常的特异性和功能特性。整体折叠是天冬氨酸转氨酶和相关的B6酶的折叠,但它也具有特定的功能。与加巴奎林(一种底物类似物)形成的复合物的结构出乎意料地表明,底物结合位点涉及分子N末端结构域的残基,尤其是Arg-32。

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