1AY2

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

1AY2 の概要

• エントリーDOI: 10.2210/pdb1ay2/pdb
• 分子名称: TYPE 4 PILIN, alpha-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose, PLATINUM (II) ION, ... (5 entities in total)
• 機能のキーワード: type iv pilin, fiber-forming protein, membrane protein, dna inding protein, contractile protein, cell adhesion
• 由来する生物種: Neisseria gonorrhoeae
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17919.10

構造登録者

Forest, K.T.,Parge, H.E.,Tainer, J.A. (登録日: 1997-11-13, 公開日: 1998-04-29, 最終更新日: 2024-11-13)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.6 Å)