1fr5
From Proteopedia
(New page: 200px<br /><applet load="1fr5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fr5, resolution 3.5Å" /> '''PHAGE FR CAPSIDS WITH...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1fr5.gif|left|200px]]<br /><applet load="1fr5" size=" | + | [[Image:1fr5.gif|left|200px]]<br /><applet load="1fr5" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1fr5, resolution 3.5Å" /> | caption="1fr5, resolution 3.5Å" /> | ||
'''PHAGE FR CAPSIDS WITH A FOUR RESIDUE DELETION IN THE COAT PROTEIN FG LOOP'''<br /> | '''PHAGE FR CAPSIDS WITH A FOUR RESIDUE DELETION IN THE COAT PROTEIN FG LOOP'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The loop between beta-strands F and G in the coat protein of small RNA | + | The loop between beta-strands F and G in the coat protein of small RNA bacteriophages forms the interactions at the fivefold and threefold (quasi-sixfold) icosahedral axes. In many cases, mutations in this region renders the coat protein unable to form capsids. This FG loop has therefore been suggested to be of major importance for the virus assembly process by guiding the assembly and helping to define the correct curvature of the virus shell. We have determined the crystal structure of a phage fr capsid where the coat protein has a four-residue deletion in the FG loop. This mutant retains the ability to form virus capsids of normal size but has a significantly lower temperature stability than the wild type. The structure reveals that the mutated loops are flexible and too short to interact with each other. This seems incompatible with a role of the FG loop in the regulation of capsid size. |
==About this Structure== | ==About this Structure== | ||
| - | 1FR5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_fr Enterobacteria phage fr]. Full crystallographic information is available from [http:// | + | 1FR5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_fr Enterobacteria phage fr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FR5 OCA]. |
==Reference== | ==Reference== | ||
| Line 23: | Line 23: | ||
[[Category: viral coat protein]] | [[Category: viral coat protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:41:45 2008'' |
Revision as of 10:41, 21 February 2008
|
PHAGE FR CAPSIDS WITH A FOUR RESIDUE DELETION IN THE COAT PROTEIN FG LOOP
Overview
The loop between beta-strands F and G in the coat protein of small RNA bacteriophages forms the interactions at the fivefold and threefold (quasi-sixfold) icosahedral axes. In many cases, mutations in this region renders the coat protein unable to form capsids. This FG loop has therefore been suggested to be of major importance for the virus assembly process by guiding the assembly and helping to define the correct curvature of the virus shell. We have determined the crystal structure of a phage fr capsid where the coat protein has a four-residue deletion in the FG loop. This mutant retains the ability to form virus capsids of normal size but has a significantly lower temperature stability than the wild type. The structure reveals that the mutated loops are flexible and too short to interact with each other. This seems incompatible with a role of the FG loop in the regulation of capsid size.
About this Structure
1FR5 is a Single protein structure of sequence from Enterobacteria phage fr. Full crystallographic information is available from OCA.
Reference
Structure of phage fr capsids with a deletion in the FG loop: implications for viral assembly., Axblom C, Tars K, Fridborg K, Orna L, Bundule M, Liljas L, Virology. 1998 Sep 15;249(1):80-8. PMID:9740779
Page seeded by OCA on Thu Feb 21 12:41:45 2008
