1ija
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(New page: 200px<br /><applet load="1ija" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ija" /> '''Structure of Sortase'''<br /> ==Overview== ...)
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Revision as of 19:58, 24 November 2007
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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
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