2vvd: Difference between revisions
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==Crystal structure of the receptor binding domain of the spike protein P1 from bacteriophage PM2== | ==Crystal structure of the receptor binding domain of the spike protein P1 from bacteriophage PM2== | ||
<StructureSection load='2vvd' size='340' side='right' caption='[[2vvd]], [[Resolution|resolution]] 2.26Å' scene=''> | <StructureSection load='2vvd' size='340' side='right'caption='[[2vvd]], [[Resolution|resolution]] 2.26Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2vvd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Alteromonas_phage_pm2 Alteromonas phage pm2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VVD OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[2vvd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Alteromonas_phage_pm2 Alteromonas phage pm2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VVD OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2VVD FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2vve|2vve]], [[2w0c|2w0c]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2vve|2vve]], [[2w0c|2w0c]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2vvd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vvd OCA], [http://pdbe.org/2vvd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vvd RCSB], [http://www.ebi.ac.uk/pdbsum/2vvd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vvd ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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</div> | </div> | ||
<div class="pdbe-citations 2vvd" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 2vvd" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Sandbox 3001|Sandbox 3001]] | |||
*[[Spike protein|Spike protein]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Alteromonas phage pm2]] | [[Category: Alteromonas phage pm2]] | ||
[[Category: Large Structures]] | |||
[[Category: Abrescia, N G.A]] | [[Category: Abrescia, N G.A]] | ||
[[Category: Assenberg, R]] | [[Category: Assenberg, R]] | ||
Revision as of 11:33, 25 June 2020
Crystal structure of the receptor binding domain of the spike protein P1 from bacteriophage PM2Crystal structure of the receptor binding domain of the spike protein P1 from bacteriophage PM2
Structural highlights
Function[SPIKE_BPPM2] Receptor binding protein located at the fivefold vertices. Publication Abstract from PubMedRecent, primarily structural observations indicate that related viruses, harboring no sequence similarity, infect hosts of different domains of life. One such clade of viruses, defined by common capsid architecture and coat protein fold, is the so-called PRD1-adenovirus lineage. Here we report the structure of the marine lipid-containing bacteriophage PM2 determined by crystallographic analyses of the entire approximately 45 MDa virion and of the outer coat proteins P1 and P2, revealing PM2 to be a primeval member of the PRD1-adenovirus lineage with an icosahedral shell and canonical double beta barrel major coat protein. The view of the lipid bilayer, richly decorated with membrane proteins, constitutes a rare visualization of an in vivo membrane. The viral membrane proteins P3 and P6 are organized into a lattice, suggesting a possible assembly pathway to produce the mature virus. Insights into virus evolution and membrane biogenesis from the structure of the marine lipid-containing bacteriophage PM2.,Abrescia NG, Grimes JM, Kivela HM, Assenberg R, Sutton GC, Butcher SJ, Bamford JK, Bamford DH, Stuart DI Mol Cell. 2008 Sep 5;31(5):749-61. PMID:18775333[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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