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| | ==Crystal structure of PilF type IV pilus assembly ATPase from Thermus thermophilus== | | ==Crystal structure of PilF type IV pilus assembly ATPase from Thermus thermophilus== |
| - | <StructureSection load='5oiu' size='340' side='right' caption='[[5oiu]], [[Resolution|resolution]] 2.44Å' scene=''> | + | <StructureSection load='5oiu' size='340' side='right'caption='[[5oiu]], [[Resolution|resolution]] 2.44Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5oiu]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Thet8 Thet8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OIU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OIU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5oiu]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OIU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OIU FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</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]] 2.44Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TTHA0364 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=300852 THET8])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=5oiu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oiu OCA], [http://pdbe.org/5oiu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5oiu RCSB], [http://www.ebi.ac.uk/pdbsum/5oiu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5oiu 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=5oiu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oiu OCA], [https://pdbe.org/5oiu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5oiu RCSB], [https://www.ebi.ac.uk/pdbsum/5oiu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5oiu 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: Thet8]] | + | [[Category: Large Structures]] |
| - | [[Category: Derrick, J P]] | + | [[Category: Thermus thermophilus HB8]] |
| - | [[Category: Karuppiah, V]] | + | [[Category: Derrick JP]] |
| - | [[Category: Aaa+]] | + | [[Category: Karuppiah V]] |
| - | [[Category: Atp]]
| + | |
| - | [[Category: Atpase]]
| + | |
| - | [[Category: Dna binding protein]]
| + | |
| - | [[Category: Motor 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 are responsible for a diverse range of functions, including twitching motility and cell adhesion. Assembly of the pilus fiber is driven by a cytoplasmic ATPase: it interacts with an inner membrane complex of biogenesis proteins which, in turn, bind to nascent pilin subunits and mediate fiber assembly. Here we report the structural characterization of the PilF TFP assembly ATPase from Thermus thermophilus. The crystal structure of a recombinant C-terminal fragment of PilF revealed bound, unhydrolysed ATP, although the full length complex was enzymatically active. 3D reconstructions were carried out by single particle cryoelectron microscopy for full length apoprotein PilF and in complex with AMPPNP. The structure forms an hourglass-like shape, with the ATPase domains in one half and the N1 domains in the second half which, we propose, interact with the other pilus biogenesis components. Molecular models for both forms were generated: binding of AMPPNP causes an upward shift of the N1 domains towards the ATPase domains of ~8 A. We advocate a model in which ATP hydrolysis is linked to displacement of the N1 domains which is associated with lifting pilin subunits out of the inner membrane, and provide the activation energy needed to form the pilus fiber.
Structural cycle of the Thermus thermophilus PilF ATPase: the powering of type IVa pilus assembly.,Collins R, Karuppiah V, Siebert CA, Dajani R, Thistlethwaite A, Derrick JP Sci Rep. 2018 Sep 19;8(1):14022. doi: 10.1038/s41598-018-32218-3. PMID:30232337[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
- ↑ Collins R, Karuppiah V, Siebert CA, Dajani R, Thistlethwaite A, Derrick JP. Structural cycle of the Thermus thermophilus PilF ATPase: the powering of type IVa pilus assembly. Sci Rep. 2018 Sep 19;8(1):14022. doi: 10.1038/s41598-018-32218-3. PMID:30232337 doi:http://dx.doi.org/10.1038/s41598-018-32218-3
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