This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1fr5

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 06:04, 9 August 2023

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

Structural highlights

1fr5 is a 3 chain structure with sequence from Enterobacteria phage fr. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.5Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CAPSD_BPFR Capsid protein self-assembles to form an icosahedral capsid with a T=3 symmetry, about 26 nm in diameter, and consisting of 89 capsid proteins dimers (178 capsid proteins). Involved in viral genome encapsidation through the interaction between a capsid protein dimer and the multiple packaging signals present in the RNA genome. The capsid contains also 1 copy of the A2 maturation protein.[UniProtKB:P03612] Acts as a translational repressor of viral replicase synthesis late in infection. This latter function is the result of capsid protein interaction with an RNA hairpin which contains the replicase ribosome-binding site.[UniProtKB:P03612]

Publication Abstract from PubMed

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.

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

↑ Axblom C, Tars K, Fridborg K, Orna L, Bundule M, Liljas L. Structure of phage fr capsids with a deletion in the FG loop: implications for viral assembly. Virology. 1998 Sep 15;249(1):80-8. PMID:9740779 doi:S0042-6822(98)99279-0

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1fr5"

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1fr5]] is a 3 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/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'>[https://proteopedia.org/fgij/fg.htm?mol=1fr5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fr5 OCA], [https://pdbe.org/1fr5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fr5 RCSB], [https://www.ebi.ac.uk/pdbsum/1fr5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fr5 ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.5&#8491;</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fr5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fr5 OCA], [https://pdbe.org/1fr5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fr5 RCSB], [https://www.ebi.ac.uk/pdbsum/1fr5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fr5 ProSAT]</span></td></tr>
 </table>
 == Function ==

1fr5

From Proteopedia

Revision as of 06:04, 9 August 2023

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

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox