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1ay2

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[[Image:1ay2.gif|left|200px]]
 
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{{Structure
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==STRUCTURE OF THE FIBER-FORMING PROTEIN PILIN AT 2.6 ANGSTROMS RESOLUTION==
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|PDB= 1ay2 |SIZE=350|CAPTION= <scene name='initialview01'>1ay2</scene>, resolution 2.6&Aring;
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<StructureSection load='1ay2' size='340' side='right'caption='[[1ay2]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CH3:METHYL+GROUP'>CH3</scene>, <scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</scene>, <scene name='pdbligand=HTO:HEPTANE-1,2,3-TRIOL'>HTO</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PT:PLATINUM+(II)+ION'>PT</scene>
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<table><tr><td colspan='2'>[[1ay2]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AY2 FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</scene>, <scene name='pdbligand=HTO:HEPTANE-1,2,3-TRIOL'>HTO</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PT:PLATINUM+(II)+ION'>PT</scene></td></tr>
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|GENE=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ay2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ay2 OCA], [https://pdbe.org/1ay2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ay2 RCSB], [https://www.ebi.ac.uk/pdbsum/1ay2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ay2 ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<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.ebi.ac.uk/pdbsum/1ay2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ay2 RCSB]</span>
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[https://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.
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}}
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ay/1ay2_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ay2 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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'''STRUCTURE OF THE FIBER-FORMING PROTEIN PILIN AT 2.6 ANGSTROMS RESOLUTION'''
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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<ref>PMID:7477282</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1ay2" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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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*[[Pilin 3D structures|Pilin 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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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].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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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]
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[[Category: Neisseria gonorrhoeae]]
[[Category: Neisseria gonorrhoeae]]
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[[Category: Single protein]]
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[[Category: Forest KT]]
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[[Category: Forest, K T.]]
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[[Category: Parge HE]]
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[[Category: Parge, H E.]]
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[[Category: Tainer JA]]
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[[Category: Tainer, J A.]]
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[[Category: fiber-forming protein]]
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[[Category: glycoprotein]]
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[[Category: saccharide]]
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[[Category: type 4 pilin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:49:46 2008''
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Current revision

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

PDB ID 1ay2

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