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| | ==C-terminal domain of capsid protein from bovine leukemia virus== | | ==C-terminal domain of capsid protein from bovine leukemia virus== |
| - | <StructureSection load='4ph1' size='340' side='right' caption='[[4ph1]], [[Resolution|resolution]] 2.46Å' scene=''> | + | <StructureSection load='4ph1' size='340' side='right'caption='[[4ph1]], [[Resolution|resolution]] 2.46Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4ph1]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Blv Blv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PH1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PH1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4ph1]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bovine_leukemia_virus Bovine leukemia virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PH1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PH1 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gag-pro-pol ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11901 BLV])</td></tr> | + | </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=4ph1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ph1 OCA], [https://pdbe.org/4ph1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ph1 RCSB], [https://www.ebi.ac.uk/pdbsum/4ph1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ph1 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ph1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ph1 OCA], [http://pdbe.org/4ph1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ph1 RCSB], [http://www.ebi.ac.uk/pdbsum/4ph1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ph1 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A7KWZ1_BLV A7KWZ1_BLV] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Blv]] | + | [[Category: Bovine leukemia virus]] |
| - | [[Category: Buschiazzo, A]] | + | [[Category: Large Structures]] |
| - | [[Category: Obal, G]] | + | [[Category: Buschiazzo A]] |
| - | [[Category: Pritsch, O]] | + | [[Category: Obal G]] |
| - | [[Category: Trajtenberg, F]] | + | [[Category: Pritsch O]] |
| - | [[Category: All alpha]]
| + | [[Category: Trajtenberg F]] |
| - | [[Category: Retroviral capsid ctd]]
| + | |
| - | [[Category: Viral protein]]
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| Structural highlights
Function
A7KWZ1_BLV
Publication Abstract from PubMed
Retroviruses depend upon self-assembly of their capsid proteins (core particle) to yield infectious mature virions. Despite the essential role of the retroviral core, its high polymorphism has hindered high-resolution structural analyses. Here, we report the x-ray structure of the native capsid (CA) protein from bovine leukemia virus. CA is organized as hexamers that deviate significantly from 6-fold symmetry, yet adjust to make two-dimensional pseudo-hexagonal arrays that mimic mature retroviral cores. Intra- and interhexameric quasi-equivalent contacts are uncovered, with flexible trimeric lateral contacts among hexamers, yet preserving very similar dimeric interfaces making the lattice. The conformation of each capsid subunit in the hexamer is therefore dictated by long-range interactions, revealing how the hexamers can also assemble into closed core particles, a relevant feature of retrovirus biology.
Conformational plasticity of a native retroviral capsid revealed by x-ray crystallography.,Obal G, Trajtenberg F, Carrion F, Tome L, Larrieux N, Zhang X, Pritsch O, Buschiazzo A Science. 2015 Jun 4. pii: aaa5182. PMID:26044299[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Obal G, Trajtenberg F, Carrion F, Tome L, Larrieux N, Zhang X, Pritsch O, Buschiazzo A. Conformational plasticity of a native retroviral capsid revealed by x-ray crystallography. Science. 2015 Jun 4. pii: aaa5182. PMID:26044299 doi:http://dx.doi.org/10.1126/science.aaa5182
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