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

被引：383

作者：

PARGE, HE ^{[1
]}

FOREST, KT ^{[1
]}

HICKEY, MJ ^{[1
]}

CHRISTENSEN, DA ^{[1
]}

GETZOFF, ED ^{[1
]}

TAINER, JA ^{[1
]}

机构：

[1] SCRIPPS RES INST, DEPT MOLEC BIOL, LA JOLLA, CA 92037 USA

来源：

NATURE | 1995年 / 378卷 / 6552期

关键词：

D O I：

10.1038/378032a0

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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 Angstrom alpha-helical spine and an O-linked disaccharide. Hey 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.

引用

页码：32 / 38

页数：7

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