1wkv

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spinqualitylabelsall models 1wkv, resolution 2.0Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of O-phosphoserine sulfhydrylase

Overview

O-Phosphoserine sulfhydrylase is a new enzyme found in a hyperthermophilic, archaeon, Aeropyrum pernix K1. This enzyme catalyzes a novel cysteine, synthetic reaction from O-phospho-l-serine and sulfide. The crystal, structure of the enzyme was determined at 2.0A resolution using the method, of multi-wavelength anomalous dispersion. A monomer consists of three, domains, including an N-terminal domain with a new alpha/beta fold. The, topology folds of the middle and C-terminal domains were similar to those, of the O-acetylserine sulfhydrylase-A from Salmonella typhimurium and the, cystathionine beta-synthase from human. The cofactor, pyridoxal, 5'-phosphate, is bound in a cleft between the middle and C-terminal, domains through a covalent linkage to Lys127. Based on the structure, determined, O-phospho-l-serine could be rationally modeled into the active, site of the enzyme. An enzyme-substrate complex model and a mutation, experiment revealed that Arg297, unique to hyperthermophilic archaea, is, one of the most crucial residues for O-phosphoserine sulfhydrylation, activity. There are more hydrophobic areas and less electric charges at, the dimer interface, compared to the S.typhimurium O-acetylserine, sulfhydrylase.

About this Structure

1WKV is a Single protein structure of sequence from Aeropyrum pernix with ACT and PLP as ligands. Full crystallographic information is available from OCA.

Reference

Three-dimensional structure of a new enzyme, O-phosphoserine sulfhydrylase, involved in l-cysteine biosynthesis by a hyperthermophilic archaeon, Aeropyrum pernix K1, at 2.0A resolution., Oda Y, Mino K, Ishikawa K, Ataka M, J Mol Biol. 2005 Aug 12;351(2):334-44. PMID:16005886

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