1fr5
From Proteopedia
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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 with sequence from [ | + | <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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.5Å</td></tr> |
| - | <table> | + | <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 == | ||
| + | [https://www.uniprot.org/uniprot/CAPSD_BPFR 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] | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
| + | <div class="pdbe-citations 1fr5" style="background-color:#fffaf0;"></div> | ||
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| + | ==See Also== | ||
| + | *[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Enterobacteria phage fr]] | [[Category: Enterobacteria phage fr]] | ||
| - | [[Category: Axblom | + | [[Category: Large Structures]] |
| - | [[Category: Bundule | + | [[Category: Axblom C]] |
| - | [[Category: Fridborg | + | [[Category: Bundule M]] |
| - | [[Category: Liljas | + | [[Category: Fridborg K]] |
| - | [[Category: Orna | + | [[Category: Liljas L]] |
| - | [[Category: Tars | + | [[Category: Orna L]] |
| - | + | [[Category: Tars K]] | |
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Current revision
PHAGE FR CAPSIDS WITH A FOUR RESIDUE DELETION IN THE COAT PROTEIN FG LOOP
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