1qwz | pdb_00001qwz

Crystal structure of Sortase B from S. aureus complexed with MTSET

spinqualitylabelsall models 1qwz, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1qwz is a 1 chain structure with sequence from Staphylococcus aureus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.75Å Ligands: ETM, NI, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SRTB_STAA8 Transpeptidase that anchors surface proteins to the cell wall (Probable) (PubMed:11830639, PubMed:15718231, PubMed:24519933). Recognizes and modifies its substrate by proteolytic cleavage of a C-terminal sorting signal. Following cleavage, a covalent intermediate is formed via a thioester bond between the sortase and its substrate, which is then transferred and covalently attached to the cell wall (Probable) (PubMed:24519933). This sortase recognizes an Asn-Pro-Gln-Thr-Asn (NPQTN) motif in IsdC, which is cleaved by the sortase between the threonine and aspargine residues; may only have 1 substrate in this bacterium (Probable). May be dedicated to the process of iron acquisition during bacterial infection (Probable). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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