Premium
The structure of a putative S‐formylglutathione hydrolase from Agrobacterium tumefaciens
Author(s) -
van Straaten Karin E.,
Gonzalez Claudio F.,
Valladares Ricardo B.,
Xu Xiaohui,
Savchenko Alexei V.,
Sanders David A. R.
Publication year - 2009
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.216
Subject(s) - agrobacterium tumefaciens , hydrolase , dimer , monomer , chemistry , enzyme , stereochemistry , crystal structure , hydrogen bond , biochemistry , crystallography , gene , molecule , transformation (genetics) , organic chemistry , polymer
The structure of the Atu1476 protein from Agrobacterium tumefaciens was determined at 2 Å resolution. The crystal structure and biochemical characterization of this enzyme support the conclusion that this protein is an S‐formylglutathione hydrolase ( Atu SFGH). The three‐dimensional structure of Atu SFGH contains the α/β 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 Atu SFGH hydrolyzes CO 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.