8e16
From Proteopedia
(Difference between revisions)
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==Mycobacterium phage Che8== | ==Mycobacterium phage Che8== | ||
| - | < | + | <SX load='8e16' size='340' side='right' viewer='molstar' caption='[[8e16]], [[Resolution|resolution]] 2.50Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[8e16]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_virus_Che8 Mycobacterium virus Che8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8E16 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8E16 FirstGlance]. <br> | <table><tr><td colspan='2'>[[8e16]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_virus_Che8 Mycobacterium virus Che8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8E16 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8E16 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=8e16 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8e16 OCA], [https://pdbe.org/8e16 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8e16 RCSB], [https://www.ebi.ac.uk/pdbsum/8e16 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8e16 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]] 2.5Å</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=8e16 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8e16 OCA], [https://pdbe.org/8e16 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8e16 RCSB], [https://www.ebi.ac.uk/pdbsum/8e16 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8e16 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 virus Che8]] | [[Category: Mycobacterium virus Che8]] | ||
[[Category: Podgorski JM]] | [[Category: Podgorski JM]] | ||
[[Category: White SJ]] | [[Category: White SJ]] | ||
Current revision
Mycobacterium phage Che8
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