The crystal structure of anthranilate phosphoribosyltransferase from the enterobacterium Pectobacterium carotovorum
The crystal structure of anthranilate phosphoribosyltransferase from the enterobacterium Pectobacterium carotovorum
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DOI：
10.1016/s0014-5793(02)02905-8
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发表时间：
2002-07-17
期刊：
影响因子：
3.5
通讯作者：
Mills, SE
中科院分区：
文献类型：
--
作者：
Kim, C;Xuong, NH;Mills, SE
来自肠杆菌Pectobacterium carotovorum的邻氨基苯甲酸磷酸核糖基转移酶的结构已经在2.4埃与Mn 2 +-焦磷酸盐复合时和在1.9埃无配体时解析。该酶的结构具有一种新的磷酸核糖基转移酶（PRT）折叠，并显示出与嘧啶核苷磷酸化酶结构的密切同源性。该酶是具有345个残基的单体的同二聚体。每个单体由两个亚结构域组成，α和α/β，它们形成包含活性位点的裂缝。从捕获的MnPPi复合物和核苷磷酸化酶的活性位点的详细知识推断活性位点的性质。随着邻氨基苯甲酸酯（An）PRT结构的解决，色氨酸生物合成所需的所有酶的结构现在都是已知的。(C)2002年由Elsevier Science B. V.代表欧洲生物化学学会联合会出版。
The structure of anthranilate phosphoribosyltransferase from the enterobacterium Pectobacterium carotovorum has been solved at 2.4 Angstrom in complex with Mn2+-pyrophosphate, and at 1.9 Angstrom without ligands. The enzyme structure has a novel phosphoribosyltransferase (PRT) fold and displays close homology to the structures of pyrimidine nucleoside phosphorylases. The enzyme is a homodimer with a monomer of 345 residues. Each monomer consists of two subdomains, alpha and alpha/beta, which form a cleft containing the active site. The nature of the active site is inferred from the trapped MnPPi complex and detailed knowledge of the active sites of nucleoside phosphorylases. With the anthranilate (An)PRT structure solved, the structures of all the enzymes required for tryptophan biosynthesis are now known. (C) 2002 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.