6m5t

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'''Unreleased structure'''
 
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The entry 6m5t is ON HOLD
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==The coordinate of the nuclease domain of the apo terminase complex==
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<StructureSection load='6m5t' size='340' side='right'caption='[[6m5t]], [[Resolution|resolution]] 2.46&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6M5T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6M5T FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.46&#8491;</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=6m5t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6m5t OCA], [https://pdbe.org/6m5t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6m5t RCSB], [https://www.ebi.ac.uk/pdbsum/6m5t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6m5t ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Genome packaging is a fundamental process in a viral life cycle and a prime target of antiviral drugs. Herpesviruses use an ATP-driven packaging motor/terminase complex to translocate and cleave concatemeric dsDNA into procapsids but its molecular architecture and mechanism are unknown. We report atomic structures of a herpesvirus hexameric terminase complex in both the apo and ADP*BeF3-bound states. Each subunit of the hexameric ring comprises three components-the ATPase/terminase pUL15 and two regulator/fixer proteins, pUL28 and pUL33-unlike bacteriophage terminases. Distal to the nuclease domains, six ATPase domains form a central channel with conserved basic-patches conducive to DNA binding and trans-acting arginine fingers are essential to ATP hydrolysis and sequential DNA translocation. Rearrangement of the nuclease domains mediated by regulatory domains converts DNA translocation mode to cleavage mode. Our structures favor a sequential revolution model for DNA translocation and suggest mechanisms for concerted domain rearrangements leading to DNA cleavage.
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Authors:
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Architecture of the herpesvirus genome-packaging complex and implications for DNA translocation.,Yang Y, Yang P, Wang N, Chen Z, Su D, Zhou ZH, Rao Z, Wang X Protein Cell. 2020 May;11(5):339-351. doi: 10.1007/s13238-020-00710-0. Epub 2020 , Apr 23. PMID:32328903<ref>PMID:32328903</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 6m5t" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Terminase 3D Structures|Terminase 3D Structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Chen ZH]]
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[[Category: Rao ZH]]
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[[Category: Wang N]]
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[[Category: Wang XX]]
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[[Category: Yang P]]
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[[Category: Yang YX]]
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[[Category: Zhou ZH]]

Current revision

The coordinate of the nuclease domain of the apo terminase complex

PDB ID 6m5t

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OCA

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