1qxa | pdb_00001qxa
Crystal structure of Sortase B complexed with Gly3
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Overview
Many surface proteins of Gram-positive bacteria, which play important, roles during the pathogenesis of human infections, are anchored to the, cell wall envelope by a mechanism requiring sortases. Sortase B, a, cysteine transpeptidase from Staphylococcus aureus, cleaves the C-terminal, sorting signal of IsdC at the NPQTN motif and tethers the polypeptide to, the pentaglycine cell wall cross-bridge. During catalysis, the active site, cysteine of sortase and the cleaved substrate form an acyl intermediate, which is then resolved by the amino group of pentaglycine cross-bridges., We report here the crystal structures of SrtBDeltaN30 in complex with two, active site inhibitors, MTSET and E64, and with the cell wall substrate, analog tripleglycine. These structures reveal, for the first time, the, active site disposition and the unique Cys-Arg catalytic machinery of the, cysteine transpeptidase, and they also provide useful information for the, future design of anti-infective agents against sortases.
About this Structure
1QXA is a Single protein structure of sequence from Staphylococcus aureus with ETM as ligand. Full crystallographic information is available from OCA.
Reference
The structure of sortase B, a cysteine transpeptidase that tethers surface protein to the Staphylococcus aureus cell wall., Zong Y, Mazmanian SK, Schneewind O, Narayana SV, Structure. 2004 Jan;12(1):105-12. PMID:14725770
Page seeded by OCA on Sun Nov 25 04:30:52 2007
