5fs4: Difference between revisions
No edit summary |
No edit summary |
||
| (4 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==Bacteriophage AP205 coat protein== | |||
<StructureSection load='5fs4' size='340' side='right'caption='[[5fs4]], [[Resolution|resolution]] 1.73Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5fs4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_phage_AP205 Acinetobacter phage AP205]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FS4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FS4 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.73Å</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=5fs4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fs4 OCA], [https://pdbe.org/5fs4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fs4 RCSB], [https://www.ebi.ac.uk/pdbsum/5fs4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fs4 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9AZ42_9VIRU Q9AZ42_9VIRU] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
AP205 is a single-stranded RNA bacteriophage that has a coat protein sequence not similar to any other known single-stranded RNA phage. Here, we report an atomic-resolution model of the AP205 virus-like particle based on a crystal structure of an unassembled coat protein dimer and a cryo-electron microscopy reconstruction of the assembled particle, together with secondary structure information from site-specific solid-state NMR data. The AP205 coat protein dimer adopts the conserved Leviviridae coat protein fold except for the N-terminal region, which forms a beta-hairpin in the other known single-stranded RNA phages. AP205 has a similar structure at the same location formed by N- and C-terminal beta-strands, making it a circular permutant compared to the other coat proteins. The permutation moves the coat protein termini to the most surface-exposed part of the assembled particle, which explains its increased tolerance to long N- and C-terminal fusions. | |||
Structure of AP205 Coat Protein Reveals Circular Permutation in ssRNA Bacteriophages.,Shishovs M, Rumnieks J, Diebolder C, Jaudzems K, Andreas LB, Stanek J, Kazaks A, Kotelovica S, Akopjana I, Pintacuda G, Koning RI, Tars K J Mol Biol. 2016 Aug 31. pii: S0022-2836(16)30345-X. doi:, 10.1016/j.jmb.2016.08.025. PMID:27591890<ref>PMID:27591890</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5fs4" style="background-color:#fffaf0;"></div> | ||
[[Category: Shishovs | |||
==See Also== | |||
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Acinetobacter phage AP205]] | |||
[[Category: Large Structures]] | |||
[[Category: Shishovs M]] | |||
[[Category: Tars K]] | |||
Latest revision as of 14:52, 9 May 2024
Bacteriophage AP205 coat proteinBacteriophage AP205 coat protein
Structural highlights
FunctionPublication Abstract from PubMedAP205 is a single-stranded RNA bacteriophage that has a coat protein sequence not similar to any other known single-stranded RNA phage. Here, we report an atomic-resolution model of the AP205 virus-like particle based on a crystal structure of an unassembled coat protein dimer and a cryo-electron microscopy reconstruction of the assembled particle, together with secondary structure information from site-specific solid-state NMR data. The AP205 coat protein dimer adopts the conserved Leviviridae coat protein fold except for the N-terminal region, which forms a beta-hairpin in the other known single-stranded RNA phages. AP205 has a similar structure at the same location formed by N- and C-terminal beta-strands, making it a circular permutant compared to the other coat proteins. The permutation moves the coat protein termini to the most surface-exposed part of the assembled particle, which explains its increased tolerance to long N- and C-terminal fusions. Structure of AP205 Coat Protein Reveals Circular Permutation in ssRNA Bacteriophages.,Shishovs M, Rumnieks J, Diebolder C, Jaudzems K, Andreas LB, Stanek J, Kazaks A, Kotelovica S, Akopjana I, Pintacuda G, Koning RI, Tars K J Mol Biol. 2016 Aug 31. pii: S0022-2836(16)30345-X. doi:, 10.1016/j.jmb.2016.08.025. PMID:27591890[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||