8eci
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 8eci is ON HOLD Authors: Podgorski, J.M., White, S.J. Description: Arthrobacter phage Bridgette Category: Unreleased Structures [[Category: Pod...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Arthrobacter phage Bridgette== | |
| + | <SX load='8eci' size='340' side='right' viewer='molstar' caption='[[8eci]], [[Resolution|resolution]] 4.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8eci]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Arthrobacter_phage_Bridgette Arthrobacter phage Bridgette]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8ECI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8ECI FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4Å</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=8eci FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8eci OCA], [https://pdbe.org/8eci PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8eci RCSB], [https://www.ebi.ac.uk/pdbsum/8eci PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8eci ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A3G2KE53_9CAUD A0A3G2KE53_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 Mar 2;31(3):282-294.e5. doi: 10.1016/j.str.2022.12.012. Epub 2023 , Jan 16. 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 8eci" style="background-color:#fffaf0;"></div> |
| - | [[Category: White | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </SX> | ||
| + | [[Category: Arthrobacter phage Bridgette]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Podgorski JM]] | ||
| + | [[Category: White SJ]] | ||
Current revision
Arthrobacter phage Bridgette
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