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4btg

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Revision as of 19:34, 25 December 2014

Coordinates of the bacteriophage phi6 capsid subunits (P1A and P1B) fitted into the cryoEM reconstruction of the procapsid at 4.4 A resolution

Structural highlights

4btg is a 2 chain structure with sequence from Pseudomonas phage phi6. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Nemecek D, Boura E, Wu W, Cheng N, Plevka P, Qiao J, Mindich L, Heymann JB, Hurley JH, Steven AC. Subunit Folds and Maturation Pathway of a dsRNA Virus Capsid. Structure. 2013 Aug 6;21(8):1374-83. doi: 10.1016/j.str.2013.06.007. Epub 2013, Jul 25. PMID:23891288 doi:10.1016/j.str.2013.06.007

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4btg"

@@ Line 5: / Line 5: @@
 </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=4btg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4btg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4btg RCSB], [http://www.ebi.ac.uk/pdbsum/4btg PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://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 ==

4btg

From Proteopedia

Revision as of 19:34, 25 December 2014

Coordinates of the bacteriophage phi6 capsid subunits (P1A and P1B) fitted into the cryoEM reconstruction of the procapsid at 4.4 A resolution

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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