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[甲基营养型细菌假单胞菌属101的NAD依赖型甲酸脱氢酶。II. 3.0埃分辨率下的酶构象]

[NAD-dependent formate dehydrogenase of methylotrophic bacteria Pseudomonas sp. 101. II. Enzyme conformation at 3.0 A resolution].

作者信息

Lamzin V S, Aleshin A E, Popov B O, Arutiunian E G

出版信息

Bioorg Khim. 1990 Mar;16(3):336-44.

PMID:2357237
Abstract

Three heavy atom isomorphous derivatives were used for the X-ray analysis of the holo form of NAD-dependent bacterial formate dehydrogenase (ternary complex enzyme-NAD-azide) at 3.0 A resolution. The enzyme subunit contains a catalytic and a coenzyme binding domain, with the active centre and the coenzyme binding site in the cleft between the domains. The polypeptide chain's fold and the position of 393 C alpha-atoms were determined. The secondary structure of the formate dehydrogenase was resolved. The structure of the NAD-binding domain is shown to be similar to that of other NAD-dependent enzymes.

摘要

使用三种重原子同晶型衍生物对NAD依赖性细菌甲酸脱氢酶(酶-NAD-叠氮化物三元复合物)的全酶形式进行了3.0埃分辨率的X射线分析。酶亚基包含一个催化结构域和一个辅酶结合结构域,活性中心和辅酶结合位点位于两个结构域之间的裂隙中。确定了多肽链的折叠方式以及393个Cα原子的位置。解析了甲酸脱氢酶的二级结构。结果表明,NAD结合结构域的结构与其他NAD依赖性酶的结构相似。

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