4bil: Difference between revisions
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==Threading model of the T7 large terminase within the gp8gp19 complex== | ==Threading model of the T7 large terminase within the gp8gp19 complex== | ||
<StructureSection load='4bil' size='340' side='right' caption='[[4bil]], [[Resolution|resolution]] 29.00Å' scene=''> | <StructureSection load='4bil' size='340' side='right' caption='[[4bil]], [[Resolution|resolution]] 29.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4bil]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[4bil]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpt7 Bpt7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BIL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BIL FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4bij|4bij]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4bij|4bij]]</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=4bil FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bil OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4bil RCSB], [http://www.ebi.ac.uk/pdbsum/4bil 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=4bil FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bil OCA], [http://pdbe.org/4bil PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4bil RCSB], [http://www.ebi.ac.uk/pdbsum/4bil PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4bil ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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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 4bil" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bpt7]] | ||
[[Category: Carrascosa, J L]] | [[Category: Carrascosa, J L]] | ||
[[Category: Dauden, M I]] | [[Category: Dauden, M I]] | ||
Revision as of 04:42, 5 August 2016
Threading model of the T7 large terminase within the gp8gp19 complexThreading model of the T7 large terminase within the gp8gp19 complex
Structural highlights
Function[VDMB_BPT7] During the growth of this phage, DNA is synthesized as concatemers. During DNA packaging mature monomers are cut from the concatemers. Gp19 is a nonspecific endonuclease that cause double stranded breaks. Its activity is suppressible by either ATP or gp18. Publication Abstract from PubMedDuring bacteriophage morphogenesis DNA is translocated into a preformed prohead by the complex formed by the portal protein, or connector, plus the terminase, which are located at an especial prohead vertex. The terminase is a powerful motor that converts ATP hydrolysis into mechanical movement of the DNA. Here, we have determined the structure of the T7 large terminase by electron microscopy. The five terminase subunits assemble in a toroid which encloses a channel wide enough to accommodate dsDNA. The structure of the complete connector/terminase complex is also reported, revealing the coupling between the terminase and the connector forming a continuous channel. The structure of the terminase assembled into the complex showed a different conformation when compared to the isolated terminase pentamer. To understand in molecular terms the terminase morphological change we generated the terminase atomic model based on the crystallographic structure of its phage T4 counterpart. The docking of the threaded model in both terminase conformations showed that the transition between the two states can be achieved by rigid body subunit rotation in the pentameric assembly. The existence of two terminase conformations and its possible relation to the sequential DNA translocation may shed light into the molecular bases of the packaging mechanism of bacteriophage T7. Large terminase conformational change induced by connector binding in bacteriophage T7.,Dauden MI, Martin-Benito J, Sanchez-Ferrero JC, Pulido-Cid M, Valpuesta JM, Carrascosa JL J Biol Chem. 2013 Apr 30. PMID:23632014[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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