1fr5: Difference between revisions
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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== | ||
<StructureSection load='1fr5' size='340' side='right' caption='[[1fr5]], [[Resolution|resolution]] 3.50Å' scene=''> | <StructureSection load='1fr5' size='340' side='right' caption='[[1fr5]], [[Resolution|resolution]] 3.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1fr5]] is a 3 chain structure | <table><tr><td colspan='2'>[[1fr5]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FR5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FR5 FirstGlance]. <br> | ||
</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=1fr5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fr5 OCA], [http://pdbe.org/1fr5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fr5 RCSB], [http://www.ebi.ac.uk/pdbsum/1fr5 PDBsum]</span></td></tr> | </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=1fr5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fr5 OCA], [http://pdbe.org/1fr5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fr5 RCSB], [http://www.ebi.ac.uk/pdbsum/1fr5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1fr5 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Axblom, C]] | [[Category: Axblom, C]] | ||
[[Category: Bundule, M]] | [[Category: Bundule, M]] | ||
Revision as of 13:50, 13 September 2017
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
Structural highlights
Function[COAT_BPFR] Forms the phage shell; binds to the phage RNA. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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