Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
