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| | == Structural highlights == | | == Structural highlights == |
| | <table><tr><td colspan='2'>[[2hi2]] 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=2HI2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HI2 FirstGlance]. <br> | | <table><tr><td colspan='2'>[[2hi2]] 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=2HI2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HI2 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HTO:HEPTANE-1,2,3-TRIOL'>HTO</scene>, <scene name='pdbligand=OPE:PHOSPHORIC+ACID+MONO-(2-AMINO-ETHYL)+ESTER'>OPE</scene>, <scene name='pdbligand=DT6:2,4-BIS(ACETYLAMINO)-2,4-DIDEOXY-BETA-D-GLUCOPYRANOSE'>DT6</scene>, <scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MEA:N-METHYLPHENYLALANINE'>MEA</scene></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DT6:2,4-BIS(ACETYLAMINO)-2,4-DIDEOXY-BETA-D-GLUCOPYRANOSE'>DT6</scene>, <scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</scene>, <scene name='pdbligand=HTO:HEPTANE-1,2,3-TRIOL'>HTO</scene>, <scene name='pdbligand=MEA:N-METHYLPHENYLALANINE'>MEA</scene>, <scene name='pdbligand=OPE:PHOSPHORIC+ACID+MONO-(2-AMINO-ETHYL)+ESTER'>OPE</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2hil|2hil]]</div></td></tr>
| + | |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2hi2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hi2 OCA], [https://pdbe.org/2hi2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hi2 RCSB], [https://www.ebi.ac.uk/pdbsum/2hi2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hi2 ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2hi2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hi2 OCA], [https://pdbe.org/2hi2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hi2 RCSB], [https://www.ebi.ac.uk/pdbsum/2hi2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hi2 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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.
| + | [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. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Neisseria gonorrhoeae]] | | [[Category: Neisseria gonorrhoeae]] |
| - | [[Category: Arvai, A S]] | + | [[Category: Arvai AS]] |
| - | [[Category: Craig, L]] | + | [[Category: Craig L]] |
| - | [[Category: Tainer, J A]] | + | [[Category: Tainer JA]] |
| - | [[Category: Cell adhesion]]
| + | |
| - | [[Category: Contractile protein]]
| + | |
| - | [[Category: Dna binding protein]]
| + | |
| - | [[Category: Fiber-forming protein]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Type iv pilin]]
| + | |
| Structural highlights
2hi2 is a 1 chain structure with sequence from Neisseria gonorrhoeae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.3Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
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 PubMed
Type IV pili (T4P) are long, thin, flexible filaments on bacteria that undergo assembly-disassembly from inner membrane pilin subunits and exhibit astonishing multifunctionality. Neisseria gonorrhoeae (gonococcal or GC) T4P are prototypic virulence factors and immune targets for increasingly antibiotic-resistant human pathogens, yet detailed structures are unavailable for any T4P. Here, we determined a detailed experimental GC-T4P structure by quantitative fitting of a 2.3 A full-length pilin crystal structure into a 12.5 A resolution native GC-T4P reconstruction solved by cryo-electron microscopy (cryo-EM) and iterative helical real space reconstruction. Spiraling three-helix bundles form the filament core, anchor the globular heads, and provide strength and flexibility. Protruding hypervariable loops and posttranslational modifications in the globular head shield conserved functional residues in pronounced grooves, creating a surprisingly corrugated pilus surface. These results clarify T4P multifunctionality and assembly-disassembly while suggesting unified assembly mechanisms for T4P, archaeal flagella, and type II secretion system filaments.
Type IV pilus structure by cryo-electron microscopy and crystallography: implications for pilus assembly and functions.,Craig L, Volkmann N, Arvai AS, Pique ME, Yeager M, Egelman EH, Tainer JA Mol Cell. 2006 Sep 1;23(5):651-62. PMID:16949362[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Craig L, Volkmann N, Arvai AS, Pique ME, Yeager M, Egelman EH, Tainer JA. Type IV pilus structure by cryo-electron microscopy and crystallography: implications for pilus assembly and functions. Mol Cell. 2006 Sep 1;23(5):651-62. PMID:16949362 doi:10.1016/j.molcel.2006.07.004
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