2bbd: Difference between revisions
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<StructureSection load='2bbd' size='340' side='right'caption='[[2bbd]], [[Resolution|resolution]] 2.04Å' scene=''> | <StructureSection load='2bbd' size='340' side='right'caption='[[2bbd]], [[Resolution|resolution]] 2.04Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2bbd]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2bbd]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulfolobus_turreted_icosahedral_virus_1 Sulfolobus turreted icosahedral virus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BBD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BBD FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.04Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2bbd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bbd OCA], [https://pdbe.org/2bbd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bbd RCSB], [https://www.ebi.ac.uk/pdbsum/2bbd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bbd ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q6Q0J0_9VIRU Q6Q0J0_9VIRU] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 2bbd" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 2bbd" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Sulfolobus turreted icosahedral virus]] | [[Category: Sulfolobus turreted icosahedral virus 1]] | ||
[[Category: Khayat | [[Category: Khayat R]] | ||
Latest revision as of 10:52, 30 October 2024
Crystal Structure of the STIV MCPCrystal Structure of the STIV MCP
Structural highlights
FunctionPublication Abstract from PubMedArchaea and their viruses are poorly understood when compared with the Eukarya and Bacteria domains of life. We report here the crystal structure of the major capsid protein (MCP) of the Sulfolobus turreted icosahedral virus, an archaeal virus isolated from an acidic hot spring (pH 2-4, 72-92 degrees C) in Yellowstone National Park. The structure is nearly identical to the MCP structures of the eukaryotic Paramecium bursaria Chlorella virus, and the bacteriophage PRD1, and shows a common fold with the mammalian adenovirus. Structural analysis of the capsid architecture, determined by fitting the subunit into the electron cryomicroscopy reconstruction of the virus, identified a number of key interactions that are akin to those observed in adenovirus and PRD1. The similar capsid proteins and capsid architectures strongly suggest that these viral capsids originated and evolved from a common ancestor. Hence, this work provides a previously undescribed example of a viral relationship spanning the three domains of life (Eukarya, Bacteria, and Archaea). The MCP structure also provides insights into the stabilizing forces required for extracellular hyperthermophilic proteins to tolerate high-temperature hot springs. Structure of an archaeal virus capsid protein reveals a common ancestry to eukaryotic and bacterial viruses.,Khayat R, Tang L, Larson ET, Lawrence CM, Young M, Johnson JE Proc Natl Acad Sci U S A. 2005 Dec 27;102(52):18944-9. Epub 2005 Dec 15. PMID:16357204[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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