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| | <StructureSection load='5it5' size='340' side='right'caption='[[5it5]], [[Resolution|resolution]] 2.65Å' scene=''> | | <StructureSection load='5it5' size='340' side='right'caption='[[5it5]], [[Resolution|resolution]] 2.65Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5it5]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/"flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IT5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5IT5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5it5]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IT5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IT5 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.648Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pilF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 "Flavobacterium thermophilum" Yoshida and Oshima 1971])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=5it5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5it5 OCA], [http://pdbe.org/5it5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5it5 RCSB], [http://www.ebi.ac.uk/pdbsum/5it5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5it5 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=5it5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5it5 OCA], [https://pdbe.org/5it5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5it5 RCSB], [https://www.ebi.ac.uk/pdbsum/5it5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5it5 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/PILB_THET8 PILB_THET8] ATPase component of the type IV pilus (T4P) that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility facilitated by cycles of extension, adhesion, and retraction of T4P fibers (By similarity) (PubMed:29717025). Acts as a molecular motor to provide the energy that is required for biogenesis of the pilus and the extrusion of substrates generated in the cytoplasm (PubMed:27667690). PilB ATPase activity is also essential for T4P extension while antagonist PilT ATPase activity is required for T4P retraction (By similarity).[UniProtKB:P22608][UniProtKB:Q1D098]<ref>PMID:27667690</ref> <ref>PMID:29717025</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Flavobacterium thermophilum yoshida and oshima 1971]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Black, W]] | + | [[Category: Thermus thermophilus]] |
| - | [[Category: Mancl, J]] | + | [[Category: Black W]] |
| - | [[Category: Robinson, H]] | + | [[Category: Mancl J]] |
| - | [[Category: Schubot, F]] | + | [[Category: Robinson H]] |
| - | [[Category: Yang, Z]] | + | [[Category: Schubot F]] |
| - | [[Category: Aaa+]]
| + | [[Category: Yang Z]] |
| - | [[Category: Atpase]]
| + | |
| - | [[Category: Hexamer]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| - | [[Category: Type iv pilus]]
| + | |
| Structural highlights
Function
PILB_THET8 ATPase component of the type IV pilus (T4P) that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility facilitated by cycles of extension, adhesion, and retraction of T4P fibers (By similarity) (PubMed:29717025). Acts as a molecular motor to provide the energy that is required for biogenesis of the pilus and the extrusion of substrates generated in the cytoplasm (PubMed:27667690). PilB ATPase activity is also essential for T4P extension while antagonist PilT ATPase activity is required for T4P retraction (By similarity).[UniProtKB:P22608][UniProtKB:Q1D098][1] [2]
Publication Abstract from PubMed
Type IV pili (T4P) mediate bacterial motility and virulence. The PilB/GspE family ATPases power the assembly of T4P and type 2 secretion systems. We determined the structure of the ATPase region of PilB (PilBATP) in complex with ATPgammaS to provide a model of a T4P assembly ATPase and a view of a PilB/GspE family hexamer at better than 3-A resolution. Spatial positioning and conformations of the protomers suggest a mechanism of force generation. All six PilBATP protomers contain bound ATPgammaS. Two protomers form a closed conformation poised for ATP hydrolysis. The other four molecules assume an open conformation but separate into two pairs with distinct active-site accessibilities. We propose that one pair represents the post-hydrolysis phase while the other pair appears poised for ADP/ATP exchange. Collectively, the data suggest that T4P assembly is powered by coordinating concurrent substrate binding with ATP hydrolysis across the PilB hexamer.
Crystal Structure of a Type IV Pilus Assembly ATPase: Insights into the Molecular Mechanism of PilB from Thermus thermophilus.,Mancl JM, Black WP, Robinson H, Yang Z, Schubot FD Structure. 2016 Sep 13. pii: S0969-2126(16)30243-X. doi:, 10.1016/j.str.2016.08.010. PMID:27667690[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Mancl JM, Black WP, Robinson H, Yang Z, Schubot FD. Crystal Structure of a Type IV Pilus Assembly ATPase: Insights into the Molecular Mechanism of PilB from Thermus thermophilus. Structure. 2016 Sep 13. pii: S0969-2126(16)30243-X. doi:, 10.1016/j.str.2016.08.010. PMID:27667690 doi:http://dx.doi.org/10.1016/j.str.2016.08.010
- ↑ Sukmana A, Yang Z. The type IV pilus assembly motor PilB is a robust hexameric ATPase with complex kinetics. Biochem J. 2018 Jun 15;475(11):1979-1993. PMID:29717025 doi:10.1042/BCJ20180167
- ↑ Mancl JM, Black WP, Robinson H, Yang Z, Schubot FD. Crystal Structure of a Type IV Pilus Assembly ATPase: Insights into the Molecular Mechanism of PilB from Thermus thermophilus. Structure. 2016 Sep 13. pii: S0969-2126(16)30243-X. doi:, 10.1016/j.str.2016.08.010. PMID:27667690 doi:http://dx.doi.org/10.1016/j.str.2016.08.010
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