1IJA

Structure of Sortase

1IJA の概要

• エントリーDOI: 10.2210/pdb1ija/pdb
• NMR情報: BMRB: 4879
• 分子名称: Sortase (1 entity in total)
• 機能のキーワード: eight stranded beta barrel, transpeptidase, protein binding
• 由来する生物種: Staphylococcus aureus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16753.00

構造登録者

Ilangovan, U.,Ton-That, H.,Iwahara, J.,Schneewind, O.,Clubb, R.T. (登録日: 2001-04-25, 公開日: 2001-05-09, 最終更新日: 2024-05-01)

主引用文献

Ilangovan, U.,Ton-That, H.,Iwahara, J.,Schneewind, O.,Clubb, R.T.
Structure of sortase, the transpeptidase that anchors proteins to the cell wall of Staphylococcus aureus.
Proc.Natl.Acad.Sci.USA, 98:6056-6061, 2001

PubMed Abstract: Surface proteins of Gram-positive bacteria play important roles during the pathogenesis of human infections and require sortase for anchoring to the cell-wall envelope. Sortase cleaves surface proteins at the LPXTG motif and catalyzes the formation of an amide bond between the carboxyl group of threonine (T) and the amino group of cell-wall crossbridges. The NMR structure of sortase reveals a unique beta-barrel structure, in which the active-site sulfhydryl of cysteine-184 is poised for ionization by histidine-120, presumably enabling the resultant thiolate to attack the LPXTG peptide. Calcium binding near the active site stimulates catalysis, possibly by altering the conformation of a surface loop that recognizes newly translocated polypeptides. The structure suggests a mechanistic relationship to the papain/cathepsin proteases and should facilitate the design of new antiinfective agents.

PubMed: 11371637
DOI: 10.1073/pnas.101064198

実験手法

SOLUTION NMR