1ay2
From Proteopedia
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[[Image:1ay2.gif|left|200px]] | [[Image:1ay2.gif|left|200px]] | ||
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'''STRUCTURE OF THE FIBER-FORMING PROTEIN PILIN AT 2.6 ANGSTROMS RESOLUTION''' | '''STRUCTURE OF THE FIBER-FORMING PROTEIN PILIN AT 2.6 ANGSTROMS RESOLUTION''' | ||
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[[Category: Parge, H E.]] | [[Category: Parge, H E.]] | ||
[[Category: Tainer, J A.]] | [[Category: Tainer, J A.]] | ||
- | [[Category: | + | [[Category: Fiber-forming protein]] |
- | [[Category: | + | [[Category: Glycoprotein]] |
- | [[Category: | + | [[Category: Saccharide]] |
- | [[Category: | + | [[Category: Type 4 pilin]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:49:50 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 07:49, 2 May 2008
STRUCTURE OF THE FIBER-FORMING PROTEIN PILIN AT 2.6 ANGSTROMS RESOLUTION
Overview
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.
About this Structure
1AY2 is a Single protein structure of sequence from Neisseria gonorrhoeae. Full crystallographic information is available from OCA.
Reference
Structure of the fibre-forming protein pilin at 2.6 A resolution., Parge HE, Forest KT, Hickey MJ, Christensen DA, Getzoff ED, Tainer JA, Nature. 1995 Nov 2;378(6552):32-8. PMID:7477282 Page seeded by OCA on Fri May 2 10:49:50 2008