This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1wkv
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1wkv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wkv, resolution 2.0Å" /> '''Crystal structure of ...)
Next diff →
Revision as of 03:22, 21 November 2007
|
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
Page seeded by OCA on Wed Nov 21 05:30:01 2007
Categories: Aeropyrum pernix | Single protein | Ataka, M. | Ishikawa, K. | Mino, K. | Oda, Y. | ACT | PLP | Homodimer | Open alpha/beta folding
