6r21
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Cryo-EM structure of T7 bacteriophage fiberless tail complex== | |
| + | <SX load='6r21' size='340' side='right' viewer='molstar' caption='[[6r21]], [[Resolution|resolution]] 3.33Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6r21]] is a 30 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=6R21 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6R21 FirstGlance]. <br> | ||
| + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6qwp|6qwp]], [[6qx5|6qx5]], [[6qxm|6qxm]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">11 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10760 BPT7]), 12 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10760 BPT7])</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=6r21 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6r21 OCA], [http://pdbe.org/6r21 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6r21 RCSB], [http://www.ebi.ac.uk/pdbsum/6r21 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6r21 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/PORTL_BPT7 PORTL_BPT7]] Forms the portal vertex of the capsid. This portal plays critical roles in head assembly, genome packaging, neck/tail attachment, and genome ejection. The portal protein multimerizes as a single ring-shaped homododecamer arranged around a central channel.[HAMAP-Rule:MF_04120]<ref>PMID:15784250</ref> <ref>PMID:23884409</ref> [[http://www.uniprot.org/uniprot/TUBE2_BPT7 TUBE2_BPT7]] Structural component of the short non-contractile tail. The tail complex is involved in viral genome delivery. Forms the end of the tail, including the canonical tube, the nozzle, and the small extensions below the fibers. Once the tail tubular structure is formed, the interface between gp11 and gp12 generates the proper environment to interact with the six gp17 trimers. [[http://www.uniprot.org/uniprot/TUBE1_BPT7 TUBE1_BPT7]] Structural component of the short non-contractile tail. The tail complex is involved in viral genome delivery. Forms the 12-fold symmetric toroidal domain immediately below the connector protein gp8. Once the tail tubular structure is formed, the interface between gp11 and gp12 generates the proper environment to interact with the six fibers, each made of gp17 trimers. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Double-stranded DNA bacteriophages package their genome at high pressure inside a procapsid through the portal, an oligomeric ring protein located at a unique capsid vertex. Once the DNA has been packaged, the tail components assemble on the portal to render the mature infective virion. The tail tightly seals the ejection conduit until infection, when its interaction with the host membrane triggers the opening of the channel and the viral genome is delivered to the host cell. Using high-resolution cryo-electron microscopy and X-ray crystallography, here we describe various structures of the T7 bacteriophage portal and fiber-less tail complex, which suggest a possible mechanism for DNA retention and ejection: a portal closed conformation temporarily retains the genome before the tail is assembled, whereas an open portal is found in the tail. Moreover, a fold including a seven-bladed beta-propeller domain is described for the nozzle tail protein. | ||
| - | + | Structures of T7 bacteriophage portal and tail suggest a viral DNA retention and ejection mechanism.,Cuervo A, Fabrega-Ferrer M, Machon C, Conesa JJ, Fernandez FJ, Perez-Luque R, Perez-Ruiz M, Pous J, Vega MC, Carrascosa JL, Coll M Nat Commun. 2019 Aug 20;10(1):3746. doi: 10.1038/s41467-019-11705-9. PMID:31431626<ref>PMID:31431626</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6r21" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </SX> | ||
| + | [[Category: Bpt7]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Carrascosa, J L]] | ||
| + | [[Category: Coll, M]] | ||
| + | [[Category: Conesa, J J]] | ||
| + | [[Category: Cuervo, A]] | ||
| + | [[Category: Fabrega-Ferrer, M]] | ||
| + | [[Category: Machon, C]] | ||
| + | [[Category: Perez-Ruiz, M]] | ||
| + | [[Category: Dna ejection]] | ||
| + | [[Category: Viral complex]] | ||
| + | [[Category: Viral protein]] | ||
Revision as of 23:58, 6 March 2020
Cryo-EM structure of T7 bacteriophage fiberless tail complex
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