4an5: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older editNewer edit →
No edit summary
No edit summary
Line 1: Line 1:
[[Image:4an5.jpg|left|200px]]
==Capsid structure and its Stability at the Late Stages of Bacteriophage SPP1 Assembly==
<StructureSection load='4an5' size='340' side='right' caption='[[4an5]], [[Resolution|resolution]] 8.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4an5]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpspp Bpspp]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AN5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AN5 FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4an5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4an5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4an5 RCSB], [http://www.ebi.ac.uk/pdbsum/4an5 PDBsum]</span></td></tr>
<table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The structure of the bacteriophage SPP1 capsid was determined at subnanometer resolution by cryo-electron microscopy and single-particle analysis. The icosahedral capsid is composed of the major capsid protein gp13 and the auxiliary protein gp12, which are organized in a T=7 lattice. DNA is arranged in layers with a distance of ~24.5 A. gp12 forms spikes that are anchored at the center of gp13 hexamers. In a gp12-deficient mutant, the centers of hexamers are closed by loops of gp13 coming together to protect the SPP1 genome from the outside environment. The HK97-like fold was used to build a pseudoatomic model of gp13. Its structural organization remains unchanged upon tail binding and following DNA release. gp13 exhibits enhanced thermostability in the DNA-filled capsid. A remarkable convergence between the thermostability of the capsid and those of the other virion components was found, revealing that the overall architecture of the SPP1 infectious particle coevolved toward high robustness.


{{STRUCTURE_4an5|  PDB=4an5  |  SCENE=  }}
Capsid structure and its stability at the late stages of bacteriophage SPP1 assembly.,White HE, Sherman MB, Brasiles S, Jacquet E, Seavers P, Tavares P, Orlova EV J Virol. 2012 Jun;86(12):6768-77. Epub 2012 Apr 18. PMID:22514336<ref>PMID:22514336</ref>


===Capsid structure and its Stability at the Late Stages of Bacteriophage SPP1 Assembly===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_22514336}}
== References ==
 
<references/>
==About this Structure==
__TOC__
[[4an5]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_phage_spp1 Bacillus phage spp1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AN5 OCA].
</StructureSection>
 
[[Category: Bpspp]]
==Reference==
<ref group="xtra">PMID:022514336</ref><references group="xtra"/>
[[Category: Bacillus phage spp1]]
[[Category: Brasiles, S.]]
[[Category: Brasiles, S.]]
[[Category: Jacquet, E.]]
[[Category: Jacquet, E.]]

Revision as of 12:25, 11 June 2014

Capsid structure and its Stability at the Late Stages of Bacteriophage SPP1 AssemblyCapsid structure and its Stability at the Late Stages of Bacteriophage SPP1 Assembly

Structural highlights

4an5 is a 7 chain structure with sequence from Bpspp. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, RCSB, PDBsum

Publication Abstract from PubMed

The structure of the bacteriophage SPP1 capsid was determined at subnanometer resolution by cryo-electron microscopy and single-particle analysis. The icosahedral capsid is composed of the major capsid protein gp13 and the auxiliary protein gp12, which are organized in a T=7 lattice. DNA is arranged in layers with a distance of ~24.5 A. gp12 forms spikes that are anchored at the center of gp13 hexamers. In a gp12-deficient mutant, the centers of hexamers are closed by loops of gp13 coming together to protect the SPP1 genome from the outside environment. The HK97-like fold was used to build a pseudoatomic model of gp13. Its structural organization remains unchanged upon tail binding and following DNA release. gp13 exhibits enhanced thermostability in the DNA-filled capsid. A remarkable convergence between the thermostability of the capsid and those of the other virion components was found, revealing that the overall architecture of the SPP1 infectious particle coevolved toward high robustness.

Capsid structure and its stability at the late stages of bacteriophage SPP1 assembly.,White HE, Sherman MB, Brasiles S, Jacquet E, Seavers P, Tavares P, Orlova EV J Virol. 2012 Jun;86(12):6768-77. Epub 2012 Apr 18. PMID:22514336[1]

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

References

  1. ↑ White HE, Sherman MB, Brasiles S, Jacquet E, Seavers P, Tavares P, Orlova EV. Capsid structure and its stability at the late stages of bacteriophage SPP1 assembly. J Virol. 2012 Jun;86(12):6768-77. Epub 2012 Apr 18. PMID:22514336 doi:10.1128/JVI.00412-12

4an5, resolution 8.80Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=4an5&oldid=1952021"