4btg: Difference between revisions
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New page: '''Unreleased structure''' The entry 4btg is ON HOLD Authors: Nemecek, D., Boura, E., Wu, W., Cheng, N., Plevka, P., Qiao, J., Mindich, L., Heymann, J.B., Hurley, J.H., Steven, A.C. De... |
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The | ==Coordinates of the bacteriophage phi6 capsid subunits (P1A and P1B) fitted into the cryoEM reconstruction of the procapsid at 4.4 A resolution== | ||
<SX load='4btg' size='340' side='right' viewer='molstar' caption='[[4btg]], [[Resolution|resolution]] 4.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4btg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_virus_phi6 Pseudomonas virus phi6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BTG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BTG FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.4Å</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4btg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4btg OCA], [https://pdbe.org/4btg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4btg RCSB], [https://www.ebi.ac.uk/pdbsum/4btg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4btg ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/P1_BPPH6 P1_BPPH6] P1 is the major inner capsid (core) protein of the polyhedral procapsid, which is responsible for genomic replication and transcription. Forms a dodecahedral shell from 60 asymmetric dimers. Binds to RNA and may be involved in genomic packaging. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The cystovirus varphi6 shares several distinct features with other double-stranded RNA (dsRNA) viruses, including the human pathogen, rotavirus: segmented genomes, nonequivalent packing of 120 subunits in its icosahedral capsid, and capsids as compartments for transcription and replication. varphi6 assembles as a dodecahedral procapsid that undergoes major conformational changes as it matures into the spherical capsid. We determined the crystal structure of the capsid protein, P1, revealing a flattened trapezoid subunit with an alpha-helical fold. We also solved the procapsid with cryo-electron microscopy to comparable resolution. Fitting the crystal structure into the procapsid disclosed substantial conformational differences between the two P1 conformers. Maturation via two intermediate states involves remodeling on a similar scale, besides huge rigid-body rotations. The capsid structure and its stepwise maturation that is coupled to sequential packaging of three RNA segments sets the cystoviruses apart from other dsRNA viruses as a dynamic molecular machine. | |||
Subunit Folds and Maturation Pathway of a dsRNA Virus Capsid.,Nemecek D, Boura E, Wu W, Cheng N, Plevka P, Qiao J, Mindich L, Heymann JB, Hurley JH, Steven AC Structure. 2013 Aug 6;21(8):1374-83. doi: 10.1016/j.str.2013.06.007. Epub 2013, Jul 25. PMID:23891288<ref>PMID:23891288</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4btg" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</SX> | |||
[[Category: Large Structures]] | |||
[[Category: Pseudomonas virus phi6]] | |||
[[Category: Boura E]] | |||
[[Category: Cheng N]] | |||
[[Category: Heymann JB]] | |||
[[Category: Hurley JH]] | |||
[[Category: Mindich L]] | |||
[[Category: Nemecek D]] | |||
[[Category: Plevka P]] | |||
[[Category: Qiao J]] | |||
[[Category: Steven AC]] | |||
[[Category: Wu W]] | |||
Latest revision as of 11:05, 9 May 2024
Coordinates of the bacteriophage phi6 capsid subunits (P1A and P1B) fitted into the cryoEM reconstruction of the procapsid at 4.4 A resolution
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