1AY2

STRUCTURE OF THE FIBER-FORMING PROTEIN PILIN AT 2.6 ANGSTROMS RESOLUTION

Summary for 1AY2

• Entry DOI: 10.2210/pdb1ay2/pdb
• Descriptor: TYPE 4 PILIN, alpha-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose, PLATINUM (II) ION, ... (5 entities in total)
• Functional Keywords: type iv pilin, fiber-forming protein, membrane protein, dna inding protein, contractile protein, cell adhesion
• Biological source: Neisseria gonorrhoeae
• Total number of polymer chains: 1
• Total formula weight: 17919.10

Authors

Forest, K.T.,Parge, H.E.,Tainer, J.A. (deposition date: 1997-11-13, release date: 1998-04-29, Last modification date: 2024-11-13)

Primary citation

Parge, H.E.,Forest, K.T.,Hickey, M.J.,Christensen, D.A.,Getzoff, E.D.,Tainer, J.A.
Structure of the fibre-forming protein pilin at 2.6 A resolution.
Nature, 378:32-38, 1995

PubMed 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.

PubMed: 7477282
DOI: 10.1038/378032a0

Experimental method

X-RAY DIFFRACTION (2.6 Å)