3E4D

Structural and Kinetic Study of an S-Formylglutathione Hydrolase from Agrobacterium tumefaciens

Summary for 3E4D

• Entry DOI: 10.2210/pdb3e4d/pdb
• Descriptor: Esterase D, MAGNESIUM ION, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: s-formylglutathione hydrolase, hydrolase fold family, catalytic triad, kinetics, proposed reaction mechanism, hydrolase
• Biological source: Agrobacterium tumefaciens
• Total number of polymer chains: 6
• Total formula weight: 192115.83

Authors

Van Straaten, K.E.,Gonzalez, C.F.,Valladares, R.B.,Xu, X.,Savchenko, A.V.,Sanders, D.A.R. (deposition date: 2008-08-11, release date: 2009-08-18, Last modification date: 2024-11-20)

Primary citation

van Straaten, K.E.,Gonzalez, C.F.,Valladares, R.B.,Xu, X.,Savchenko, A.V.,Sanders, D.A.
The structure of a putative S-formylglutathione hydrolase from Agrobacterium tumefaciens
Protein Sci., 18:2196-2202, 2009

PubMed 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.

PubMed: 19653299
DOI: 10.1002/pro.216

Experimental method

X-RAY DIFFRACTION (2.01 Å)