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| <StructureSection load='6okv' size='340' side='right'caption='[[6okv]], [[Resolution|resolution]] 4.01Å' scene=''> | | <StructureSection load='6okv' size='340' side='right'caption='[[6okv]], [[Resolution|resolution]] 4.01Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[6okv]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Geomg Geomg]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OKV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OKV FirstGlance]. <br> | | <table><tr><td colspan='2'>[[6okv]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacter_metallireducens_GS-15 Geobacter metallireducens GS-15]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OKV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OKV FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 4.007Å</td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6ok2|6ok2]], [[6ojz|6ojz]], [[6ojy|6ojy]], [[6ojx|6ojx]]</td></tr> | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pilT-4, Gmet_1394 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=269799 GEOMG])</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=6okv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6okv OCA], [https://pdbe.org/6okv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6okv RCSB], [https://www.ebi.ac.uk/pdbsum/6okv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6okv ProSAT]</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=6okv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6okv OCA], [http://pdbe.org/6okv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6okv RCSB], [http://www.ebi.ac.uk/pdbsum/6okv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6okv ProSAT]</span></td></tr> | |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
| | == Function == |
| == Publication Abstract from PubMed == | | [https://www.uniprot.org/uniprot/Q39VU6_GEOMG Q39VU6_GEOMG] |
| Type IV pilus-like systems are protein complexes that polymerize pilin fibres. They are critical for virulence in many bacterial pathogens. Pilin polymerization and depolymerization are powered by motor ATPases of the PilT/VirB11-like family. This family is thought to operate with C2 symmetry; however, most of these ATPases crystallize with either C3 or C6 symmetric conformations. The relevance of these conformations is unclear. Here, we determine the X-ray structures of PilT in four unique conformations and use these structures to classify the conformation of available PilT/VirB11-like family member structures. Single particle electron cryomicroscopy (cryoEM) structures of PilT reveal condition-dependent preferences for C2, C3, and C6 conformations. The physiologic importance of these conformations is validated by coevolution analysis and functional studies of point mutants, identifying a rare gain-of-function mutation that favours the C2 conformation. With these data, we propose a comprehensive model of PilT function with broad implications for PilT/VirB11-like family members.
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| Multiple conformations facilitate PilT function in the type IV pilus.,McCallum M, Benlekbir S, Nguyen S, Tammam S, Rubinstein JL, Burrows LL, Howell PL Nat Commun. 2019 Nov 15;10(1):5198. doi: 10.1038/s41467-019-13070-z. PMID:31729381<ref>PMID:31729381</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 6okv" style="background-color:#fffaf0;"></div>
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| == References ==
| |
| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Geomg]] | | [[Category: Geobacter metallireducens GS-15]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Howell, P L]] | | [[Category: Howell PL]] |
| [[Category: McCallum, M]] | | [[Category: McCallum M]] |
| [[Category: Atpase]]
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| [[Category: Motor]]
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| [[Category: Motor protein]]
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| [[Category: T4p]]
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| [[Category: Type iv pilus]]
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