1ay2
STRUCTURE OF THE FIBER-FORMING PROTEIN PILIN AT 2.6 ANGSTROMS RESOLUTION
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OverviewOverview
The crystallographic structure of Neisseria gonorrhoeae pilin, which, assembles into the multifunctional pilus adhesion and virulence factor, reveals an alpha-beta roll fold with a striking 85 A alpha-helical spine, and an O-linked disaccharide. Key residues stabilize interactions that, allow sequence hypervariability, responsible for pilin's celebrated, antigenic variation, within disulphide region beta-strands and, connections. Pilin surface shape, hydrophobicity and sequence variation, constrain pilus assembly to the packing of flat subunit faces against, alpha 1 helices. Helical fibre assembly is postulated to form a core of, coiled alpha 1 helices banded by beta-sheet, leaving carbohydrate and, hypervariable sequence regions exposed to solvent.
About this StructureAbout this Structure
1AY2 is a Single protein structure of sequence from Neisseria gonorrhoeae with PT and HTO as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Structure of the fibre-forming protein pilin at 2.6 A resolution., Parge HE, Forest KT, Hickey MJ, Christensen DA, Getzoff ED, Tainer JA, Nature. 1995 Nov 2;378(6552):32-8. PMID:7477282
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