6ok2: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<StructureSection load='6ok2' size='340' side='right'caption='[[6ok2]], [[Resolution|resolution]] 3.29Å' scene=''> | <StructureSection load='6ok2' size='340' side='right'caption='[[6ok2]], [[Resolution|resolution]] 3.29Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6ok2]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OK2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OK2 FirstGlance]. <br> | <table><tr><td colspan='2'>[[6ok2]] 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=6OK2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OK2 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></td></tr> | </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> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6ojz|6ojz]], [[6ojy|6ojy]], [[6ojx|6ojx]], [[6okv|6okv]], [[6olj|6olj]], [[6olm|6olm]], [[6oll|6oll]], [[6olk|6olk]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6ojz|6ojz]], [[6ojy|6ojy]], [[6ojx|6ojx]], [[6okv|6okv]], [[6olj|6olj]], [[6olm|6olm]], [[6oll|6oll]], [[6olk|6olk]]</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ok2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ok2 OCA], [http://pdbe.org/6ok2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ok2 RCSB], [http://www.ebi.ac.uk/pdbsum/6ok2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ok2 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=6ok2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ok2 OCA], [http://pdbe.org/6ok2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ok2 RCSB], [http://www.ebi.ac.uk/pdbsum/6ok2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ok2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6ok2" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Geomg]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Howell, P L]] | [[Category: Howell, P L]] | ||
Revision as of 09:07, 27 November 2019
PilT4 from Geobacter metallireducens bound to ADP: C3ocococ conformation
| ||||||||||||
