1WKV

Crystal structure of O-phosphoserine sulfhydrylase

1WKV の概要

• エントリーDOI: 10.2210/pdb1wkv/pdb
• 分子名称: cysteine synthase, ACETATE ION, PYRIDOXAL-5'-PHOSPHATE, ... (4 entities in total)
• 機能のキーワード: homodimer, open alpha/beta folding, transferase
• 由来する生物種: Aeropyrum pernix
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 84664.08

構造登録者

Oda, Y.,Mino, K.,Ishikawa, K.,Ataka, M. (登録日: 2004-06-09, 公開日: 2005-06-28, 最終更新日: 2025-03-26)

主引用文献

Oda, Y.,Mino, K.,Ishikawa, K.,Ataka, M.
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
J.Mol.Biol., 351:334-344, 2005

PubMed Abstract: 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.

PubMed: 16005886
DOI: 10.1016/j.jmb.2005.05.064

実験手法

X-RAY DIFFRACTION (2 Å)