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| <StructureSection load='7jq7' size='340' side='right'caption='[[7jq7]], [[Resolution|resolution]] 2.90Å' scene=''> | | <StructureSection load='7jq7' size='340' side='right'caption='[[7jq7]], [[Resolution|resolution]] 2.90Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[7jq7]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactococcus_lactis_phage_asccphi28 Lactococcus lactis phage asccphi28]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7JQ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7JQ7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7JQ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7JQ7 FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.895Å</td></tr> |
- | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <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"><div style='overflow: auto; max-height: 3em;'>[[7jq6|7jq6]]</div></td></tr>
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| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7jq7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7jq7 OCA], [https://pdbe.org/7jq7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7jq7 RCSB], [https://www.ebi.ac.uk/pdbsum/7jq7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7jq7 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=7jq7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7jq7 OCA], [https://pdbe.org/7jq7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7jq7 RCSB], [https://www.ebi.ac.uk/pdbsum/7jq7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7jq7 ProSAT]</span></td></tr> |
| </table> | | </table> |
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Lactococcus lactis phage asccphi28]] | |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Dill, E]] | + | [[Category: Dill E]] |
- | [[Category: Morais, M C]] | + | [[Category: Morais MC]] |
- | [[Category: White, M A]] | + | [[Category: White MA]] |
- | [[Category: Asce fold]]
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- | [[Category: Atpase]]
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- | [[Category: Dna packaging]]
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- | [[Category: Motor]]
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- | [[Category: Phage]]
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- | [[Category: Viral protein]]
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| Structural highlights
Publication Abstract from PubMed
Double-stranded DNA viruses package their genomes into pre-assembled capsids using virally-encoded ASCE ATPase ring motors. We present the first atomic-resolution crystal structure of a multimeric ring form of a viral dsDNA packaging motor, the ATPase of the asccphi28 phage, and characterize its atomic-level dynamics via long timescale molecular dynamics simulations. Based on these results, and previous single-molecule data and cryo-EM reconstruction of the homologous phi29 motor, we propose an overall packaging model that is driven by helical-to-planar transitions of the ring motor. These transitions are coordinated by inter-subunit interactions that regulate catalytic and force-generating events. Stepwise ATP binding to individual subunits increase their affinity for the helical DNA phosphate backbone, resulting in distortion away from the planar ring towards a helical configuration, inducing mechanical strain. Subsequent sequential hydrolysis events alleviate the accumulated mechanical strain, allowing a stepwise return of the motor to the planar conformation, translocating DNA in the process. This type of helical-to-planar mechanism could serve as a general framework for ring ATPases.
Atomistic basis of force generation, translocation, and coordination in a viral genome packaging motor.,Pajak J, Dill E, Reyes-Aldrete E, White MA, Kelch BA, Jardine PJ, Arya G, Morais MC Nucleic Acids Res. 2021 May 29. pii: 6288440. doi: 10.1093/nar/gkab372. PMID:34050764[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Pajak J, Dill E, Reyes-Aldrete E, White MA, Kelch BA, Jardine PJ, Arya G, Morais MC. Atomistic basis of force generation, translocation, and coordination in a viral genome packaging motor. Nucleic Acids Res. 2021 May 29. pii: 6288440. doi: 10.1093/nar/gkab372. PMID:34050764 doi:http://dx.doi.org/10.1093/nar/gkab372
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