来自根癌土壤杆菌的一种假定的S-甲酰谷胱甘肽水解酶的结构。
The structure of a putative S-formylglutathione hydrolase from Agrobacterium tumefaciens.
作者信息
van Straaten Karin E, Gonzalez Claudio F, Valladares Ricardo B, Xu Xiaohui, Savchenko Alexei V, Sanders David A R
机构信息
Department of Chemistry, University of Saskatchewan, Saskatoon, SK, Canada.
出版信息
Protein Sci. 2009 Oct;18(10):2196-202. doi: 10.1002/pro.216.
Abstract
The structure of the Atu1476 protein from Agrobacterium tumefaciens was determined at 2 A resolution. The crystal structure and biochemical characterization of this enzyme support the conclusion that this protein is an S-formylglutathione hydrolase (AtuSFGH). The three-dimensional structure of AtuSFGH contains the alpha/beta hydrolase fold topology and exists as a homo-dimer. Contacts between the two monomers in the dimer are formed both by hydrogen bonds and salt bridges. Biochemical characterization reveals that AtuSFGH hydrolyzes C--O bonds with high affinity toward short to medium chain esters, unlike the other known SFGHs which have greater affinity toward shorter chained esters. A potential role for Cys54 in regulation of enzyme activity through S-glutathionylation is also proposed.
摘要
根癌农杆菌Atu1476蛋白的结构在2埃分辨率下得以确定。该酶的晶体结构和生化特性支持这一结论：此蛋白是一种S-甲酰谷胱甘肽水解酶（AtuSFGH）。AtuSFGH的三维结构包含α/β水解酶折叠拓扑结构，且以同型二聚体形式存在。二聚体中两个单体之间的接触通过氢键和盐桥形成。生化特性表明，AtuSFGH对短至中链酯具有高亲和力来水解C-O键，这与其他已知的对短链酯具有更高亲和力的SFGH不同。还提出了半胱氨酸54在通过S-谷胱甘肽化调节酶活性方面的潜在作用。
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