1H4M

Sulfurtransferase from Azotobacter vinelandii in complex with phosphate

1H4M の概要

• エントリーDOI: 10.2210/pdb1h4m/pdb
• 関連するPDBエントリー: 1E0C 1H4K
• 分子名称: PUTATIVE THIOSULFATE SULFURTRANSFERASE, 1,2-ETHANEDIOL (3 entities in total)
• 機能のキーワード: transferase, sulfur metabolism, thiosulfate:cyanide
• 由来する生物種: AZOTOBACTER VINELANDII
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29788.55

構造登録者

Bordo, D.,Forlani, F.,Spallarossa, A.,Colnaghi, R.,Carpen, A.,Pagani, S.,Bolognesi, M. (登録日: 2001-05-11, 公開日: 2002-05-16, 最終更新日: 2023-12-13)

主引用文献

Bordo, D.,Forlani, F.,Spallarossa, A.,Colnaghi, R.,Carpen, A.,Bolognesi, M.,Pagani, S.
A Persulfurated Cysteine Promotes Active Site Reactivity in Azotobacter Vinelandii Rhodanse
Biol.Chem., 382:1245-, 2001

PubMed Abstract: Active site reactivity and specificity of RhdA, a thiosulfate:cyanide sulfurtransferase (rhodanese) from Azotobacter vinelandii, have been investigated through ligand binding, site-directed mutagenesis, and X-ray crystallographic techniques, in a combined approach. In native RhdA the active site Cys230 is found persulfurated; fluorescence and sulfurtransferase activity measurements show that phosphate anions interact with Cys230 persulfide sulfur atom and modulate activity. Crystallographic analyses confirm that phosphate and hypophosphite anions react with native RhdA, removing the persulfide sulfur atom from the active site pocket. Considering that RhdA and the catalytic subunit of Cdc25 phosphatases share a common three-dimensional fold as well as active site Cys (catalytic) and Arg residues, two RhdA mutants carrying a single amino acid insertion at the active site loop were designed and their phosphatase activity tested. The crystallographic and functional results reported here show that specific sulfurtransferase or phosphatase activities are strictly related to precise tailoring of the catalytic loop structure in RhdA and Cdc25 phosphatase, respectively.

PubMed: 11592406
DOI: 10.1515/BC.2001.155

実験手法

X-RAY DIFFRACTION (2.1 Å)