5hd9: Difference between revisions
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<StructureSection load='5hd9' size='340' side='right'caption='[[5hd9]], [[Resolution|resolution]] 1.94Å' scene=''> | <StructureSection load='5hd9' size='340' side='right'caption='[[5hd9]], [[Resolution|resolution]] 1.94Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5hd9]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5hd9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_virus_phi29 Bacillus virus phi29]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HD9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HD9 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.941Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5hd9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hd9 OCA], [https://pdbe.org/5hd9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hd9 RCSB], [https://www.ebi.ac.uk/pdbsum/5hd9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hd9 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/PKG16_BPPH2 PKG16_BPPH2] ATPase required for the genome encapsidation reaction. Part of the active packaging motor via the binding to the packaging RNA (pRNA), itself fixed to the head-tail connector at the unique portal vertex of the prohead. Binds and supercoils the DNA-gp3 to produce an initiation complex for DNA packaging. Provides the energy to actively pump the viral DNA into the prohead. Approximately one molecule of ATP is used in the packaging of 2 bp of viral DNA. After packaging, the ATPase and the pRNA are released from the prohead.<ref>PMID:11130079</ref> <ref>PMID:18674782</ref> <ref>PMID:2960820</ref> <ref>PMID:3879485</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: | [[Category: Bacillus virus phi29]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Mao | [[Category: Mao H]] | ||
[[Category: Morais | [[Category: Morais MC]] | ||
[[Category: Reyes-Aldrete | [[Category: Reyes-Aldrete E]] | ||
Latest revision as of 10:32, 9 August 2023
Crystal Structure of the N-terminal domain of the DNA packaging ATPase from bacteriophage phi29Crystal Structure of the N-terminal domain of the DNA packaging ATPase from bacteriophage phi29
Structural highlights
FunctionPKG16_BPPH2 ATPase required for the genome encapsidation reaction. Part of the active packaging motor via the binding to the packaging RNA (pRNA), itself fixed to the head-tail connector at the unique portal vertex of the prohead. Binds and supercoils the DNA-gp3 to produce an initiation complex for DNA packaging. Provides the energy to actively pump the viral DNA into the prohead. Approximately one molecule of ATP is used in the packaging of 2 bp of viral DNA. After packaging, the ATPase and the pRNA are released from the prohead.[1] [2] [3] [4] Publication Abstract from PubMedRing NTPases are a class of ubiquitous molecular motors involved in basic biological partitioning processes. dsDNA viruses encode ring ATPases that translocate their genomes to near-crystalline densities within pre-assembled viral capsids. Here, X-ray crystallography, cryoEM, and biochemical analyses of the dsDNA packaging motor in bacteriophage phi29 show how individual subunits are arranged in a pentameric ATPase ring and suggest how their activities are coordinated to translocate dsDNA. The resulting pseudo-atomic structure of the motor and accompanying functional analyses show how ATP is bound in the ATPase active site; identify two DNA contacts, including a potential DNA translocating loop; demonstrate that a trans-acting arginine finger is involved in coordinating hydrolysis around the ring; and suggest a functional coupling between the arginine finger and the DNA translocating loop. The ability to visualize the motor in action illuminates how the different motor components interact with each other and with their DNA substrate. Structural and Molecular Basis for Coordination in a Viral DNA Packaging Motor.,Mao H, Saha M, Reyes-Aldrete E, Sherman MB, Woodson M, Atz R, Grimes S, Jardine PJ, Morais MC Cell Rep. 2016 Mar 1;14(8):2017-29. doi: 10.1016/j.celrep.2016.01.058. Epub 2016 , Feb 18. PMID:26904950[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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