8eco
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Microbacterium phage Oxtober96== | |
| + | <StructureSection load='8eco' size='340' side='right'caption='[[8eco]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8eco]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Microbacterium_phage_Oxtober96 Microbacterium phage Oxtober96]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8ECO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8ECO 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=8eco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8eco OCA], [https://pdbe.org/8eco PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8eco RCSB], [https://www.ebi.ac.uk/pdbsum/8eco PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8eco ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A6G8R1V0_9CAUD A0A6G8R1V0_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 8eco" style="background-color:#fffaf0;"></div> |
| - | [[Category: White | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Microbacterium phage Oxtober96]] | ||
| + | [[Category: Podgorski JM]] | ||
| + | [[Category: White SJ]] | ||
Revision as of 11:22, 1 February 2023
Microbacterium phage Oxtober96
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