8ecj
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Mycobacterium phage Cain== | |
| + | <StructureSection load='8ecj' size='340' side='right'caption='[[8ecj]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8ecj]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_phage_Cain Mycobacterium phage Cain]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8ECJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8ECJ 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=8ecj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ecj OCA], [https://pdbe.org/8ecj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ecj RCSB], [https://www.ebi.ac.uk/pdbsum/8ecj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ecj ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A222ZM90_9CAUD A0A222ZM90_9CAUD] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Many double-stranded DNA viruses, including tailed bacteriophages (phages) and herpesviruses, use the HK97-fold in their major capsid protein to make the capsomers of the icosahedral viral capsid. After the genome packaging at near-crystalline densities, the capsid is subjected to a major expansion and stabilization step that allows it to withstand environmental stresses and internal high pressure. Several different mechanisms for stabilizing the capsid have been structurally characterized, but how these mechanisms have evolved is still not understood. Using cryo-EM structure determination of 10 capsids, structural comparisons, phylogenetic analyses, and Alphafold predictions, we have constructed a detailed structural dendrogram describing the evolution of capsid structural stability within the actinobacteriophages. We show that the actinobacteriophage major capsid proteins can be classified into 15 groups based upon their HK97-fold. | ||
| - | + | A structural dendrogram of the actinobacteriophage major capsid proteins provides important structural insights into the evolution of capsid stability.,Podgorski JM, Freeman K, Gosselin S, Huet A, Conway JF, Bird M, Grecco J, Patel S, Jacobs-Sera D, Hatfull G, Gogarten JP, Ravantti J, White SJ Structure. 2023 Jan 7:S0969-2126(22)00498-1. doi: 10.1016/j.str.2022.12.012. PMID:36649709<ref>PMID:36649709</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Podgorski | + | <div class="pdbe-citations 8ecj" style="background-color:#fffaf0;"></div> |
| - | [[Category: White | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mycobacterium phage Cain]] | ||
| + | [[Category: Podgorski JM]] | ||
| + | [[Category: White SJ]] | ||
Revision as of 11:22, 1 February 2023
Mycobacterium phage Cain
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