3zn6: Difference between revisions

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New page: '''Unreleased structure''' The entry 3zn6 is ON HOLD Authors: Rissanen, I., Grimes, J.M., Pawlowski, A., Mantynen, S., Harlos, K., Bamford, J.K.H., Stuart, D.I. Description: VP16-VP17 ...
 
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'''Unreleased structure'''


The entry 3zn6 is ON HOLD
==VP16-VP17 complex, a complex of the two major capsid proteins of bacteriophage P23-77==
<StructureSection load='3zn6' size='340' side='right'caption='[[3zn6]], [[Resolution|resolution]] 1.53&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3zn6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_virus_P23-77 Thermus virus P23-77]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZN6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZN6 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.53&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=3zn6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zn6 OCA], [https://pdbe.org/3zn6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zn6 RCSB], [https://www.ebi.ac.uk/pdbsum/3zn6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zn6 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/C8CHL4_9VIRU C8CHL4_9VIRU]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
It has proved difficult to classify viruses unless they are closely related since their rapid evolution hinders detection of remote evolutionary relationships in their genetic sequences. However, structure varies more slowly than sequence, allowing deeper evolutionary relationships to be detected. Bacteriophage P23-77 is an example of a newly identified viral lineage, with members inhabiting extreme environments. We have solved multiple crystal structures of the major capsid proteins VP16 and VP17 of bacteriophage P23-77. They fit the 14 A resolution cryo-electron microscopy reconstruction of the entire virus exquisitely well, allowing us to propose a model for both the capsid architecture and viral assembly, quite different from previously published models. The structures of the capsid proteins and their mode of association to form the viral capsid suggest that the P23-77-like and adeno-PRD1 lineages of viruses share an extremely ancient common ancestor.


Authors: Rissanen, I., Grimes, J.M., Pawlowski, A., Mantynen, S., Harlos, K., Bamford, J.K.H., Stuart, D.I.
Bacteriophage p23-77 capsid protein structures reveal the archetype of an ancient branch from a major virus lineage.,Rissanen I, Grimes JM, Pawlowski A, Mantynen S, Harlos K, Bamford JK, Stuart DI Structure. 2013 May 7;21(5):718-26. doi: 10.1016/j.str.2013.02.026. Epub 2013 Apr, 25. PMID:23623731<ref>PMID:23623731</ref>


Description: VP16-VP17 complex, a complex of the two major capsid proteins of bacteriophage P23-77
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3zn6" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermus virus P23-77]]
[[Category: Bamford JKH]]
[[Category: Grimes JM]]
[[Category: Harlos K]]
[[Category: Mantynen S]]
[[Category: Pawlowski A]]
[[Category: Rissanen I]]
[[Category: Stuart DI]]

Latest revision as of 14:06, 20 December 2023

VP16-VP17 complex, a complex of the two major capsid proteins of bacteriophage P23-77VP16-VP17 complex, a complex of the two major capsid proteins of bacteriophage P23-77

Structural highlights

3zn6 is a 2 chain structure with sequence from Thermus virus P23-77. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.53Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

C8CHL4_9VIRU

Publication Abstract from PubMed

It has proved difficult to classify viruses unless they are closely related since their rapid evolution hinders detection of remote evolutionary relationships in their genetic sequences. However, structure varies more slowly than sequence, allowing deeper evolutionary relationships to be detected. Bacteriophage P23-77 is an example of a newly identified viral lineage, with members inhabiting extreme environments. We have solved multiple crystal structures of the major capsid proteins VP16 and VP17 of bacteriophage P23-77. They fit the 14 A resolution cryo-electron microscopy reconstruction of the entire virus exquisitely well, allowing us to propose a model for both the capsid architecture and viral assembly, quite different from previously published models. The structures of the capsid proteins and their mode of association to form the viral capsid suggest that the P23-77-like and adeno-PRD1 lineages of viruses share an extremely ancient common ancestor.

Bacteriophage p23-77 capsid protein structures reveal the archetype of an ancient branch from a major virus lineage.,Rissanen I, Grimes JM, Pawlowski A, Mantynen S, Harlos K, Bamford JK, Stuart DI Structure. 2013 May 7;21(5):718-26. doi: 10.1016/j.str.2013.02.026. Epub 2013 Apr, 25. PMID:23623731[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Rissanen I, Grimes JM, Pawlowski A, Mantynen S, Harlos K, Bamford JK, Stuart DI. Bacteriophage p23-77 capsid protein structures reveal the archetype of an ancient branch from a major virus lineage. Structure. 2013 May 7;21(5):718-26. doi: 10.1016/j.str.2013.02.026. Epub 2013 Apr, 25. PMID:23623731 doi:10.1016/j.str.2013.02.026

3zn6, resolution 1.53Å

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