4ncd

Crystal Structure of Class 5 Fimbriae Chaperone CfaA

spinqualitylabelsall models 4ncd, resolution 2.04Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ncd is a 1 chain structure with sequence from Escherichia coli P0301867.5. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Adhesive pili on the surface of pathogenic bacteria comprise polymerized pilin subunits and are essential for initiation of infections. Pili assembled by the chaperone-usher pathway (CUP) require periplasmic chaperones that assist subunit folding, maintain their stability, and escort them to the site of bioassembly. Until now, CUP chaperones have been classified into two families, FGS and FGL, based on the short and long length of the subunit-interacting loops between its F1 and G1 beta-strands, respectively. CfaA is the chaperone for assembly of colonization factor antigen I (CFA/I) pili of enterotoxigenic E. coli (ETEC), a cause of diarrhea in travelers and young children. Here, the crystal structure of CfaA along with sequence analyses reveals some unique structural and functional features, leading us to propose a separate family for CfaA and closely related chaperones. Phenotypic changes resulting from mutations in regions unique to this chaperone family provide insight into their function, consistent with involvement of these regions in interactions with cognate subunits and usher proteins during pilus assembly. Structure of CfaA Suggests a New Family of Chaperones Essential for Assembly of Class 5 Fimbriae.,Bao R, Fordyce A, Chen YX, McVeigh A, Savarino SJ, Xia D PLoS Pathog. 2014 Aug 14;10(8):e1004316. doi: 10.1371/journal.ppat.1004316., eCollection 2014 Aug. PMID:25122114 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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