This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1ay2
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1ay2.gif|left|200px]] | [[Image:1ay2.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1ay2", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | | | + | or leave the SCENE parameter empty for the default display. |
| - | | | + | --> |
| - | + | {{STRUCTURE_1ay2| PDB=1ay2 | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''STRUCTURE OF THE FIBER-FORMING PROTEIN PILIN AT 2.6 ANGSTROMS RESOLUTION''' | '''STRUCTURE OF THE FIBER-FORMING PROTEIN PILIN AT 2.6 ANGSTROMS RESOLUTION''' | ||
| Line 28: | Line 25: | ||
[[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
