1ay2: Difference between revisions
New page: left|200px<br /><applet load="1ay2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ay2, resolution 2.6Å" /> '''STRUCTURE OF THE FIBE... |
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[[Image:1ay2.gif|left|200px]]<br /><applet load="1ay2" size=" | [[Image:1ay2.gif|left|200px]]<br /><applet load="1ay2" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1ay2, resolution 2.6Å" /> | caption="1ay2, resolution 2.6Å" /> | ||
'''STRUCTURE OF THE FIBER-FORMING PROTEIN PILIN AT 2.6 ANGSTROMS RESOLUTION'''<br /> | '''STRUCTURE OF THE FIBER-FORMING PROTEIN PILIN AT 2.6 ANGSTROMS RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
The crystallographic structure of Neisseria gonorrhoeae pilin, which | 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== | ==About this Structure== | ||
1AY2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Neisseria_gonorrhoeae Neisseria gonorrhoeae] with PT and HTO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1AY2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Neisseria_gonorrhoeae Neisseria gonorrhoeae] with <scene name='pdbligand=PT:'>PT</scene> and <scene name='pdbligand=HTO:'>HTO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AY2 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Neisseria gonorrhoeae]] | [[Category: Neisseria gonorrhoeae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Forest, K | [[Category: Forest, K T.]] | ||
[[Category: Parge, H | [[Category: Parge, H E.]] | ||
[[Category: Tainer, J | [[Category: Tainer, J A.]] | ||
[[Category: HTO]] | [[Category: HTO]] | ||
[[Category: PT]] | [[Category: PT]] | ||
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[[Category: type 4 pilin]] | [[Category: type 4 pilin]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:49:31 2008'' | ||
Revision as of 12:49, 21 February 2008
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STRUCTURE OF THE FIBER-FORMING PROTEIN PILIN AT 2.6 ANGSTROMS RESOLUTION
OverviewOverview
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 StructureAbout this Structure
1AY2 is a Single protein structure of sequence from Neisseria gonorrhoeae with and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
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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