1fr5: Difference between revisions

Revision as of 03:49, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1fr5.png

Template:STRUCTURE 1fr5

PHAGE FR CAPSIDS WITH A FOUR RESIDUE DELETION IN THE COAT PROTEIN FG LOOPPHAGE FR CAPSIDS WITH A FOUR RESIDUE DELETION IN THE COAT PROTEIN FG LOOP

Template:ABSTRACT PUBMED 9740779

About this StructureAbout this Structure

1FR5 is a Single protein structure of sequence from Enterobacteria phage fr. Full crystallographic information is available from OCA.

ReferenceReference

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

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-'''PHAGE FR CAPSIDS WITH A FOUR RESIDUE DELETION IN THE COAT PROTEIN FG LOOP'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_9740779}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9740779 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9740779}}
 ==About this Structure==
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 [[Category: Icosahedral virus]]
 [[Category: Viral coat protein]]
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