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'''Crystal structure of O-phosphoserine sulfhydrylase''' | '''Crystal structure of O-phosphoserine sulfhydrylase''' | ||
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[[Category: Mino, K.]] | [[Category: Mino, K.]] | ||
[[Category: Oda, Y.]] | [[Category: Oda, Y.]] | ||
[[Category: | [[Category: Homodimer]] | ||
[[Category: | [[Category: Open alpha/beta folding]] | ||
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Revision as of 10:49, 3 May 2008
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. 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 Page seeded by OCA on Sat May 3 13:49:15 2008
