4hji | pdb_00004hji

Structure of the CooA pilin subunit from enterotoxigenic Escherichia coli

spinqualitylabelsall models 4hji, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4hji is a 2 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: IMD, NA Gene: csoA, cooA ("Bacillus coli" Migula 1895) Resources: FirstGlance, OCA, RCSB, PDBsum Function [CSOA_ECOLX] Fimbriae (also called pili), polar filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300 per cell, enable bacteria to colonize the epithelium of specific host organs. Publication Abstract from PubMed Enterotoxigenic Escherichia coli (ETEC) is a bacterial pathogen that causes diarrhea in children and travelers in developing countries. ETEC adhere to host epithelial cells in the small intestine via a variety of different pili. The CS1 pilus is a prototype for a family of related pili, including the CFA/I pili, present on ETEC and other Gram-negative bacterial pathogens. These pili are assembled by an outer membrane usher protein that catalyzes subunit polymerization via donor strand complementation, in which the N-terminus of each incoming pilin subunit fits into a hydrophobic groove in the terminal subunit, completing a beta-sheet in the Ig fold. Here we determined a crystal structure of the CS1 major pilin subunit, CooA, to 1.6 A resolution. CooA is a globular protein with an Ig fold and is similar in structure to the CFA/I major pilin CfaB. We determined three distinct negative stain electron microscopic reconstructions of the CS1 pilus and generated pseudo-atomic resolution pilus structures using the CooA crystal structure. CS1 pili adopt multiple structural states with differences in subunit orientations and packing. We propose that the structural perturbations are accommodated by flexibility in the N-terminal donor strand of CooA and by plasticity in interactions between exposed flexible loops on adjacent subunits. Our results suggest that CS1 and other pili of this class are extensible filaments that can be stretched in response to mechanical stress encountered during colonization. STRUCTURE OF THE CS1 PILUS OF ENTEROTOXIGENIC ESCHERICHIA COLI REVEALS STRUCTURAL POLYMORPHISM.,Galkin VE, Kolappan S, Ng D, Zong Z, Li J, Yu X, Egelman EH, Craig L J Bacteriol. 2012 Nov 21. PMID:23175654 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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