1ija
From Proteopedia
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'''Structure of Sortase''' | '''Structure of Sortase''' | ||
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[[Category: Schneewind, O.]] | [[Category: Schneewind, O.]] | ||
[[Category: Ton-That, H.]] | [[Category: Ton-That, H.]] | ||
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- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 17:03, 2 May 2008
Structure of Sortase
Overview
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.
About this Structure
1IJA is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.
Reference
Structure of sortase, the transpeptidase that anchors proteins to the cell wall of Staphylococcus aureus., Ilangovan U, Ton-That H, Iwahara J, Schneewind O, Clubb RT, Proc Natl Acad Sci U S A. 2001 May 22;98(11):6056-61. PMID:11371637 Page seeded by OCA on Fri May 2 20:03:45 2008