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1ay2
From Proteopedia
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| - | [[Image:1ay2.gif|left|200px]] | + | [[Image:1ay2.gif|left|200px]] |
| - | + | ||
| - | '''STRUCTURE OF THE FIBER-FORMING PROTEIN PILIN AT 2.6 ANGSTROMS RESOLUTION''' | + | {{Structure |
| + | |PDB= 1ay2 |SIZE=350|CAPTION= <scene name='initialview01'>1ay2</scene>, resolution 2.6Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=PT:PLATINUM+(II)+ION'>PT</scene> and <scene name='pdbligand=HTO:HEPTANE-1,2,3-TRIOL'>HTO</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''STRUCTURE OF THE FIBER-FORMING PROTEIN PILIN AT 2.6 ANGSTROMS RESOLUTION''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1AY2 is a [ | + | 1AY2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Neisseria_gonorrhoeae Neisseria gonorrhoeae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AY2 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/7477282 7477282] |
[[Category: Neisseria gonorrhoeae]] | [[Category: Neisseria gonorrhoeae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: type 4 pilin]] | [[Category: type 4 pilin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:03:43 2008'' |
Revision as of 08:03, 20 March 2008
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| , resolution 2.6Å | |||||||
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| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Thu Mar 20 10:03:43 2008
