8ec2
From Proteopedia
(Difference between revisions)
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==Mycobacterium phage Adephagia== | ==Mycobacterium phage Adephagia== | ||
| - | < | + | <SX load='8ec2' size='340' side='right' viewer='molstar' caption='[[8ec2]], [[Resolution|resolution]] 2.40Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[8ec2]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_phage_Adephagia Mycobacterium phage Adephagia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8EC2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8EC2 FirstGlance]. <br> | <table><tr><td colspan='2'>[[8ec2]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_phage_Adephagia Mycobacterium phage Adephagia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8EC2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8EC2 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=8ec2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ec2 OCA], [https://pdbe.org/8ec2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ec2 RCSB], [https://www.ebi.ac.uk/pdbsum/8ec2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ec2 ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.4Å</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=8ec2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ec2 OCA], [https://pdbe.org/8ec2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ec2 RCSB], [https://www.ebi.ac.uk/pdbsum/8ec2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ec2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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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. | 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 | + | 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> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
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<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
| - | </ | + | </SX> |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Mycobacterium phage Adephagia]] | [[Category: Mycobacterium phage Adephagia]] | ||
[[Category: Podgorski JM]] | [[Category: Podgorski JM]] | ||
[[Category: White SJ]] | [[Category: White SJ]] | ||
Current revision
Mycobacterium phage Adephagia
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