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1wkv
From Proteopedia
| |||||||
| , resolution 2.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | APE1586 (Aeropyrum pernix) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Thu Mar 20 14:58:15 2008
Categories: Aeropyrum pernix | Single protein | Ataka, M. | Ishikawa, K. | Mino, K. | Oda, Y. | ACT | PLP | Homodimer | Open alpha/beta folding
