1URH

The "Rhodanese" fold and catalytic mechanism of 3-mercaptopyruvate sulfotransferases: Crystal structure of SseA from Escherichia coli

1URH の概要

• エントリーDOI: 10.2210/pdb1urh/pdb
• 分子名称: 3-MERCAPTOPYRUVATE SULFURTRANSFERASE, SULFITE ION (3 entities in total)
• 機能のキーワード: sulfur-transferase, rhodanese, transferase
• 由来する生物種: ESCHERICHIA COLI
• 細胞内の位置: Cytoplasm (Probable): P31142
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 61563.26

構造登録者

Spallarossa, A.,Forlani, F.,Carpen, A.,Armirotti, A.,Pagani, S.,Bolognesi, M.,Bordo, D. (登録日: 2003-10-30, 公開日: 2003-12-18, 最終更新日: 2024-11-06)

主引用文献

Spallarossa, A.,Forlani, F.,Carpen, A.,Armirotti, A.,Pagani, S.,Bolognesi, M.,Bordo, D.
The "Rhodanese" Fold and Catalytic Mechanism of 3-Mercaptopyruvate Sulfurtransferases: Crystal Structure of Ssea from Escherichia Coli
J.Mol.Biol., 335:583-, 2004

PubMed Abstract: 3-Mercaptopyruvate sulfurtransferases (MSTs) catalyze, in vitro, the transfer of a sulfur atom from substrate to cyanide, yielding pyruvate and thiocyanate as products. They display clear structural homology with the protein fold observed in the rhodanese sulfurtransferase family, composed of two structurally related domains. The role of MSTs in vivo, as well as their detailed molecular mechanisms of action have been little investigated. Here, we report the crystal structure of SseA, a MST from Escherichia coli, which is the first MST three-dimensional structure disclosed to date. SseA displays specific structural differences relative to eukaryotic and prokaryotic rhodaneses. In particular, conformational variation of the rhodanese active site loop, hosting the family invariant catalytic Cys residue, may support a new sulfur transfer mechanism involving Cys237 as the nucleophilic species and His66, Arg102 and Asp262 as residues assisting catalysis.

PubMed: 14672665
DOI: 10.1016/J.JMB.2003.10.072

実験手法

X-RAY DIFFRACTION (2.8 Å)