5it5
From Proteopedia
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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=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'>[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> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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. | ||
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| + | 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<ref>PMID:27667690</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5it5" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 11:11, 26 October 2016
Thermus thermophilus PilB core ATPase region
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Categories: Black, W | Mancl, J | Robinson, H | Schubot, F | Yang, Z | Aaa+ | Atpase | Hexamer | Transport protein | Type iv pilus
