2BHS

Crystal Structure of Cysteine Synthase B

2BHS の概要

• エントリーDOI: 10.2210/pdb2bhs/pdb
• 関連するPDBエントリー: 2BHT
• 分子名称: CYSTEINE SYNTHASE B, PYRIDOXAL-5'-PHOSPHATE (3 entities in total)
• 機能のキーワード: cysteine biosynthesis, plp-dependent enzyme, pyridoxal-5'-phosphate, pyridoxal phosphate, transferase
• 由来する生物種: ESCHERICHIA COLI
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 131784.98

構造登録者

Claus, M.T.,Zocher, G.E.,Maier, T.H.P.,Schulz, G.E. (登録日: 2005-01-18, 公開日: 2005-06-22, 最終更新日: 2011-07-13)

主引用文献

Claus, M.T.,Zocher, G.E.,Maier, T.H.P.,Schulz, G.E.
Structure of the O-Acetylserine Sulfhydrylase Isoenzyme Cysm from Escherichia Coli
Biochemistry, 44:8620-, 2005

PubMed Abstract: The enzyme O-acetylserine sulfhydrylase participates in the biosynthesis of l-cysteine in bacteria and plants. The structure of isoenzyme B (CysM) from Escherichia coli was established in a hexagonal crystal form at 2.7 A resolution (wild-type) and in a merohedrally twinned tetragonal crystal form at 2.1 A resolution (surface mutant). Structural superpositions revealed the variations with respect to isoenzyme A (CysK) and explained the different substrate specificities. A geometric model of the reaction catalyzed by CysM is proposed. Both isoenzymes are used for the production of l-amino acid derivatives as building blocks for the synthesis of peptides and peptidomimetic drugs. Since the structure of CysM revealed a remarkable main chain variation at the active center, it constitutes a further starting point for engineering mutants with novel substrate specificities.

PubMed: 15952768
DOI: 10.1021/BI050485+

実験手法

X-RAY DIFFRACTION (2.67 Å)