4d70 | pdb_00004d70

Structural, biophysical and biochemical analyses of a Clostridium perfringens Sortase D5 transpeptidase

spinqualitylabelsall models 4d70, resolution 1.99Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4d70 is a 2 chain structure with sequence from Clostridium perfringens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.99Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8XNW0_CLOPE Publication Abstract from PubMed The assembly and anchorage of various pathogenic proteins on the surface of Gram-positive bacteria is mediated by the sortase family of enzymes. These cysteine transpeptidases catalyze a unique sorting signal motif located at the C-terminus of their target substrate and promote the covalent attachment of these proteins onto an amino nucleophile located on another protein or on the bacterial cell wall. Each of the six distinct classes of sortases displays a unique biological role, with sequential activation of multiple sortases often observed in many Gram-positive bacteria to decorate their peptidoglycans. Less is known about the members of the class D family of sortases (SrtD), but they have a suggested role in spore formation in an oxygen-limiting environment. Here, the crystal structure of the SrtD enzyme from Clostridium perfringens was determined at 1.99 A resolution. Comparative analysis of the C. perfringens SrtD structure reveals the typical eight-stranded beta-barrel fold observed in all other known sortases, along with the conserved catalytic triad consisting of cysteine, histidine and arginine residues. Biochemical approaches further reveal the specifics of the SrtD catalytic activity in vitro, with a significant preference for the LPQTGS sorting motif. Additionally, the catalytic activity of SrtD is most efficient at 316 K and can be further improved in the presence of magnesium cations. Since C. perfringens spores are heat-resistant and lead to foodborne illnesses, characterization of the spore-promoting sortase SrtD may lead to the development of new antimicrobial agents. Structural and biochemical analyses of a Clostridium perfringens sortase D transpeptidase.,Suryadinata R, Seabrook SA, Adams TE, Nuttall SD, Peat TS Acta Crystallogr D Biol Crystallogr. 2015 Jul 1;71(Pt 7):1505-13. doi:, 10.1107/S1399004715009219. Epub 2015 Jun 30. PMID:26143922 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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