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6ojz

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Current revision (07:11, 11 October 2023) (edit) (undo)
 
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<StructureSection load='6ojz' size='340' side='right'caption='[[6ojz]], [[Resolution|resolution]] 3.03&Aring;' scene=''>
<StructureSection load='6ojz' size='340' side='right'caption='[[6ojz]], [[Resolution|resolution]] 3.03&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6ojz]] 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=6OJZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OJZ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6ojz]] 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=6OJZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OJZ FirstGlance]. <br>
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</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></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.027&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6ojx|6ojx]], [[6ojy|6ojy]], [[6ok2|6ok2]], [[6okv|6okv]]</td></tr>
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<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></td></tr>
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<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>
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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=6ojz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ojz OCA], [https://pdbe.org/6ojz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ojz RCSB], [https://www.ebi.ac.uk/pdbsum/6ojz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ojz ProSAT]</span></td></tr>
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<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=6ojz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ojz OCA], [http://pdbe.org/6ojz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ojz RCSB], [http://www.ebi.ac.uk/pdbsum/6ojz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ojz ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q39VU6_GEOMG Q39VU6_GEOMG]
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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&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 6ojz" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Geomg]]
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[[Category: Geobacter metallireducens GS-15]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Howell, P L]]
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[[Category: Howell PL]]
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[[Category: McCallum, M]]
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[[Category: McCallum M]]
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[[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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Current revision

PilT4 from Geobacter metallireducens bound to ADP with partial occupancy: C3ocococ conformation

PDB ID 6ojz

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