5cuw
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Crystal structure of Sortase E1 from Streptomyces coelicolor with tripeptide in the active site
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Structural highlights
FunctionSRTE1_STRCO Transpeptidase that anchors surface proteins to the cell wall. Recognizes both Leu-Ala-x-Thr-Gly and Leu-Pro-x-Thr-Gly, with a preference for the former. Unlike the S.aureus sortase it cleaves not only the Thr-Gly motif but also the Ala-X bond; Ala-Glu and Ala-His bonds are better substrates than the Thr-Gly motif in vitro (PubMed:22296345, PubMed:27936128). Among its possible substrates are the chaplins ChpA, ChpB and ChpC; this enzyme is less important for ChpC attachment than is SrtE2. A double knockout mutant of srtE1 and srtE2 shows a developmental defect in aerial hyphae formation more dramatic than that due to chaplin deletion (PubMed:22296345).[1] [2] References
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This page was last modified 12:21, 6 March 2024.