2AE3

Glutaryl 7-Aminocephalosporanic Acid Acylase: mutational study of activation mechanism

2AE3 の概要

• エントリーDOI: 10.2210/pdb2ae3/pdb
• 関連するPDBエントリー: 2ADV 2AE4 2AE5
• 分子名称: Glutaryl 7-Aminocephalosporanic Acid Acylase, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: autoproteolysis, precursor activation, intermediate structure, cephalosporin acylase, hydrolase
• 由来する生物種: Pseudomonas sp.; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 77378.75

構造登録者

Kim, J.K.,Yang, I.S.,Shin, H.J.,Cho, K.J.,Ryu, E.K.,Kim, S.H.,Park, S.S.,Kim, K.H. (登録日: 2005-07-21, 公開日: 2006-01-24, 最終更新日: 2024-03-13)

主引用文献

Kim, J.K.,Yang, I.S.,Shin, H.J.,Cho, K.J.,Ryu, E.K.,Kim, S.H.,Park, S.S.,Kim, K.H.
Insight into autoproteolytic activation from the structure of cephalosporin acylase: a protein with two proteolytic chemistries.
Proc.Natl.Acad.Sci.USA, 103:1732-1737, 2006

PubMed Abstract: Cephalosporin acylase (CA), a member of the N-terminal nucleophile hydrolase family, is activated through sequential primary and secondary autoproteolytic reactions with the release of a pro segment. We have determined crystal structures of four CA mutants. Two mutants are trapped after the primary cleavage, and the other two undergo secondary cleavage slowly. These structures provide a look at pro-segment conformation during activation in N-terminal nucleophile hydrolases. The highly strained helical pro segment of precursor is transformed into a relaxed loop in the intermediates, suggesting that the relaxation of structural constraints drives the primary cleavage reaction. The secondary autoproteolytic step has been proposed to be intermolecular. However, our analysis provides evidence that CA is processed in two sequential steps of intramolecular autoproteolysis involving two distinct residues in the active site, the first a serine and the second a glutamate.

PubMed: 16446446
DOI: 10.1073/pnas.0507862103

実験手法

X-RAY DIFFRACTION (2.4 Å)