We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1qbe

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1qbe.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1qbe.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1qbe| PDB=1qbe | SCENE= }}
{{STRUCTURE_1qbe| PDB=1qbe | SCENE= }}
-
'''BACTERIOPHAGE Q BETA CAPSID'''
+
===BACTERIOPHAGE Q BETA CAPSID===
-
==Overview==
+
<!--
-
BACKGROUND: The capsid protein subunits of small RNA bacteriophages form a T = 3 particle upon assembly and RNA encapsidation. Dimers of the capsid protein repress translation of the replicase gene product by binding to the ribosome binding site and this interaction is believed to initiate RNA encapsidation. We have determined the crystal structure of phage Q beta with the aim of clarifying which factors are the most important for particle assembly and RNA interaction in the small phages. RESULTS: The crystal structure of bacteriophage Q beta determined at 3.5 A resolution shows that the capsid is stabilized by disulfide bonds on each side of the flexible loops that are situated around the fivefold and quasi-sixfold axes. As in other small RNA phages, the protein capsid is constructed from subunits which associate into dimers. A contiguous ten-stranded antiparallel beta sheet facing the RNA is formed in the dimer. The disulfide bonds lock the constituent dimers of the capsid covalently in the T = 3 lattice. CONCLUSIONS: The unusual stability of the Q beta particle is due to the tight dimer interactions and the disulfide bonds linking each dimer covalently to the rest of the capsid. A comparison with the structure of the related phage MS2 shows that although the fold of the Q beta coat protein is very similar, the details of the protein-protein interactions are completely different. The most conserved region of the protein is at the surface, which, in MS2, is involved in RNA binding.
+
The line below this paragraph, {{ABSTRACT_PUBMED_8736553}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 8736553 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_8736553}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Icosahedral virus]]
[[Category: Icosahedral virus]]
[[Category: Rna binding]]
[[Category: Rna binding]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:05:44 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:03:00 2008''

Revision as of 16:03, 28 July 2008

Image:1qbe.png

Template:STRUCTURE 1qbe

BACTERIOPHAGE Q BETA CAPSID

Template:ABSTRACT PUBMED 8736553

About this Structure

1QBE is a Single protein structure of sequence from Enterobacteria phage qbeta. Full crystallographic information is available from OCA.

Reference

The crystal structure of bacteriophage Q beta at 3.5 A resolution., Golmohammadi R, Fridborg K, Bundule M, Valegard K, Liljas L, Structure. 1996 May 15;4(5):543-54. PMID:8736553

Page seeded by OCA on Mon Jul 28 19:03:00 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1qbe"
Personal tools