1frs: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| (7 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==CRYSTAL STRUCTURE OF BACTERIOPHAGE FR CAPSIDS AT 3.5 ANGSTROMS RESOLUTION== | ==CRYSTAL STRUCTURE OF BACTERIOPHAGE FR CAPSIDS AT 3.5 ANGSTROMS RESOLUTION== | ||
<StructureSection load='1frs' size='340' side='right' caption='[[1frs]], [[Resolution|resolution]] 3.50Å' scene=''> | <StructureSection load='1frs' size='340' side='right'caption='[[1frs]], [[Resolution|resolution]] 3.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1frs]] is a 3 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1frs]] 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=1FRS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FRS 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=1frs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1frs OCA], [https://pdbe.org/1frs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1frs RCSB], [https://www.ebi.ac.uk/pdbsum/1frs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1frs 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 == | ||
| Line 13: | Line 17: | ||
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 1frs" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 18: | Line 23: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Enterobacteria phage fr]] | [[Category: Enterobacteria phage fr]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Bundule M]] | ||
[[Category: | [[Category: Liljas L]] | ||
[[Category: | [[Category: Valegard K]] | ||
