| Literature DB >> 7477282 |
H E Parge1, K T Forest, M J Hickey, D A Christensen, E D Getzoff, J A Tainer.
Abstract
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.Entities:
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Year: 1995 PMID: 7477282 DOI: 10.1038/378032a0
Source DB: PubMed Journal: Nature ISSN: 0028-0836 Impact factor: 49.962