1ay2: Difference between revisions
No edit summary |
No edit summary |
||
| Line 7: | Line 7: | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ay2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ay2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ay2 RCSB], [http://www.ebi.ac.uk/pdbsum/1ay2 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ay2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ay2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ay2 RCSB], [http://www.ebi.ac.uk/pdbsum/1ay2 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/FMM1_NEIGO FMM1_NEIGO]] This protein is the predominant Neisseria surface antigen, which allows adhesion of the bacterium to various host cells. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 15:33, 25 December 2014
STRUCTURE OF THE FIBER-FORMING PROTEIN PILIN AT 2.6 ANGSTROMS RESOLUTIONSTRUCTURE OF THE FIBER-FORMING PROTEIN PILIN AT 2.6 ANGSTROMS RESOLUTION
Structural highlights
Function[FMM1_NEIGO] This protein is the predominant Neisseria surface antigen, which allows adhesion of the bacterium to various host cells. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||