View source for 6qzf


==The cryo-EM structure of the collar complex and tail axis in genome emptied bacteriophage phi29==
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== Structural highlights ==
<table><tr><td colspan='2'>[[6qzf]] is a 60 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_phage_phi29 Bacillus phage phi29]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QZF OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6QZF FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6qzf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qzf OCA], [http://pdbe.org/6qzf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qzf RCSB], [http://www.ebi.ac.uk/pdbsum/6qzf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qzf ProSAT]</span></td></tr>
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== Function ==
[[http://www.uniprot.org/uniprot/PORTL_BPPH2 PORTL_BPPH2]] Forms the portal vertex of the capsid (PubMed:10801350) (PubMed:19744688, PubMed:21570409). This portal plays critical roles in head assembly, genome packaging, neck/tail attachment, and genome ejection (By similarity). The portal protein multimerizes as a single ring-shaped homododecamer arranged around a central channel (PubMed:11812138, PubMed:21570409). Binds to the 6 packaging RNA molecules (pRNA) forming a double-ring structure which in turn binds to the ATPase gp16 hexamer, forming the active DNA-translocating motor (PubMed:15886394, PubMed:11130079). This complex is essential for the specificity of packaging from the left DNA end.[UniProtKB:P13334]<ref>PMID:11130079</ref> <ref>PMID:11812138</ref> <ref>PMID:15886394</ref> <ref>PMID:19744688</ref> <ref>PMID:21570409</ref> <ref>PMID:10801350</ref>  [[http://www.uniprot.org/uniprot/FIB12_BPPH2 FIB12_BPPH2]] Structural component of the 12 appendages that hang from the lower collar. Adhesion protein that binds to the host cell surface during virus attachment and mediates teichoic acids degradation.<ref>PMID:7241648</ref>  [[http://www.uniprot.org/uniprot/TUB11_BPPH2 TUB11_BPPH2]] Forms the proximal part of the tail tube.<ref>PMID:6096227</ref>  
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== Publication Abstract from PubMed ==
The mature virion of the tailed bacteriophage varphi29 is an ~33 MDa complex that contains more than 450 subunits of seven structural proteins assembling into a prolate head and a short non-contractile tail. Here, we report the near-atomic structures of the varphi29 pre-genome packaging head (prohead), the mature virion and the genome-emptied virion. Structural comparisons suggest local rotation or oscillation of the head-tail connector upon DNA packaging and release. Termination of the DNA packaging occurs through pressure-dependent correlative positional and conformational changes in the connector. The funnel-shaped tail lower collar attaches the expanded narrow end of the connector and has a 180-A long, 24-strand beta barrel narrow stem tube that undergoes conformational changes upon genome release. The appendages form an interlocked assembly attaching the tail around the collar. The membrane active long loops at the distal end of the tail knob exit during the late stage of infection and form the cone-shaped tip of a largely hydrophobic helix barrel, prepared for membrane penetration.

Structural assembly of the tailed bacteriophage varphi29.,Xu J, Wang D, Gui M, Xiang Y Nat Commun. 2019 May 30;10(1):2366. doi: 10.1038/s41467-019-10272-3. PMID:31147544<ref>PMID:31147544</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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[[Category: Bacillus phage phi29]]
[[Category: Large Structures]]
[[Category: Gui, M]]
[[Category: Wang, D]]
[[Category: Xiang, Y]]
[[Category: Xu, J]]
[[Category: Bacteriophage]]
[[Category: Genome emptied virion]]
[[Category: Phi29]]
[[Category: Virus]]