Structure of the fibre-forming protein pilin at 2.6 A resolution.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 7477282.
- No licence information is recorded for this record.
- Because redistribution is not established, this page shows the abstract only. Follow the links below for the full text.
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.