4znk: Difference between revisions
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==Thermus Phage P74-26 Large Terminase ATPase domain from (P 32 2 1 space group)== | ==Thermus Phage P74-26 Large Terminase ATPase domain from (P 32 2 1 space group)== | ||
<StructureSection load='4znk' size='340' side='right' caption='[[4znk]], [[Resolution|resolution]] 1.93Å' scene=''> | <StructureSection load='4znk' size='340' side='right' caption='[[4znk]], [[Resolution|resolution]] 1.93Å' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4zni|4zni]], [[4znj|4znj]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4zni|4zni]], [[4znj|4znj]]</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=4znk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4znk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4znk RCSB], [http://www.ebi.ac.uk/pdbsum/4znk PDBsum]</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=4znk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4znk OCA], [http://pdbe.org/4znk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4znk RCSB], [http://www.ebi.ac.uk/pdbsum/4znk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4znk ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4znk" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 16:24, 10 May 2017
Thermus Phage P74-26 Large Terminase ATPase domain from (P 32 2 1 space group)Thermus Phage P74-26 Large Terminase ATPase domain from (P 32 2 1 space group)
Structural highlights
Publication Abstract from PubMedMany viruses package their genomes into procapsids using an ATPase machine that is among the most powerful known biological motors. However, how this motor couples ATP hydrolysis to DNA translocation is still unknown. Here, we introduce a model system with unique properties for studying motor structure and mechanism. We describe crystal structures of the packaging motor ATPase domain that exhibit nucleotide-dependent conformational changes involving a large rotation of an entire subdomain. We also identify the arginine finger residue that catalyzes ATP hydrolysis in a neighboring motor subunit, illustrating that previous models for motor structure need revision. Our findings allow us to derive a structural model for the motor ring, which we validate using small-angle X-ray scattering and comparisons with previously published data. We illustrate the model's predictive power by identifying the motor's DNA-binding and assembly motifs. Finally, we integrate our results to propose a mechanistic model for DNA translocation by this molecular machine. Structure and mechanism of the ATPase that powers viral genome packaging.,Hilbert BJ, Hayes JA, Stone NP, Duffy CM, Sankaran B, Kelch BA Proc Natl Acad Sci U S A. 2015 Jul 21;112(29):E3792-9. doi:, 10.1073/pnas.1506951112. Epub 2015 Jul 6. PMID:26150523[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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