1ay2

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[[Image:1ay2.gif|left|200px]]
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{{STRUCTURE_1ay2| PDB=1ay2 | SCENE= }}
{{STRUCTURE_1ay2| PDB=1ay2 | SCENE= }}
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'''STRUCTURE OF THE FIBER-FORMING PROTEIN PILIN AT 2.6 ANGSTROMS RESOLUTION'''
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===STRUCTURE OF THE FIBER-FORMING PROTEIN PILIN AT 2.6 ANGSTROMS RESOLUTION===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_7477282}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 7477282 is the PubMed ID number.
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{{ABSTRACT_PUBMED_7477282}}
==About this Structure==
==About this Structure==
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[[Category: Saccharide]]
[[Category: Saccharide]]
[[Category: Type 4 pilin]]
[[Category: Type 4 pilin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:49:50 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:50:23 2008''

Revision as of 14:50, 30 June 2008

Template:STRUCTURE 1ay2

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

Template:ABSTRACT PUBMED 7477282

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

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