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==Structure of a Spumaretrovirus Gag central domain reveals an ancient retroviral capsid== | ==Structure of a Spumaretrovirus Gag central domain reveals an ancient retroviral capsid== | ||
<StructureSection load='5m1h' size='340' side='right' caption='[[5m1h | <StructureSection load='5m1h' size='340' side='right'caption='[[5m1h]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5m1h]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M1H OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5m1h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_spumaretrovirus Human spumaretrovirus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M1H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5M1H FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=5m1h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m1h OCA], [https://pdbe.org/5m1h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5m1h RCSB], [https://www.ebi.ac.uk/pdbsum/5m1h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5m1h ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/GAG_FOAMV GAG_FOAMV] Involved in capsid formation and genome binding. Shortly after infection, interaction between incoming particle-associated Gag proteins and host dynein allows centrosomal targeting of the viral genome (associated to Gag), prior to nucleus translocation and integration into host genome.<ref>PMID:16160174</ref> <ref>PMID:12857789</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
The Spumaretrovirinae, or | The Spumaretrovirinae, or foamy viruses (FVs) are complex retroviruses that infect many species of monkey and ape. Despite little sequence homology, FV and orthoretroviral Gag proteins perform equivalent functions, including genome packaging, virion assembly, trafficking and membrane targeting. However, there is a paucity of structural information for FVs and it is unclear how disparate FV and orthoretroviral Gag molecules share the same function. To probe the functional overlap of FV and orthoretroviral Gag we have determined the structure of a central region of Gag from the Prototype FV (PFV). The structure comprises two all alpha-helical domains NtDCEN and CtDCEN that although they have no sequence similarity, we show they share the same core fold as the N- (NtDCA) and C-terminal domains (CtDCA) of archetypal orthoretroviral capsid protein (CA). Moreover, structural comparisons with orthoretroviral CA align PFV NtDCEN and CtDCEN with NtDCA and CtDCA respectively. Further in vitro and functional virological assays reveal that residues making inter-domain NtDCEN-CtDCEN interactions are required for PFV capsid assembly and that intact capsid is required for PFV reverse transcription. These data provide the first information that relates the Gag proteins of Spuma and Orthoretrovirinae and suggests a common ancestor for both lineages containing an ancient CA fold. | ||
Structure of a Spumaretrovirus Gag Central Domain Reveals an Ancient Retroviral Capsid.,Ball NJ, Nicastro G, Dutta M, Pollard DJ, Goldstone DC, Sanz-Ramos M, Ramos A, Mullers E, Stirnnagel K, Stanke N, Lindemann D, Stoye JP, Taylor WR, Rosenthal PB, Taylor IA PLoS Pathog. 2016 Nov 9;12(11):e1005981. doi: 10.1371/journal.ppat.1005981., eCollection 2016 Nov. PMID:27829070<ref>PMID:27829070</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> | ||
</div> | </div> | ||
<div class="pdbe-citations 5m1h" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5m1h" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Gag polyprotein 3D structures|Gag polyprotein 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Human spumaretrovirus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Ball N]] | ||
[[Category: | [[Category: Nicastro G]] | ||
[[Category: | [[Category: Taylor IA]] | ||
Latest revision as of 21:19, 1 November 2023
Structure of a Spumaretrovirus Gag central domain reveals an ancient retroviral capsidStructure of a Spumaretrovirus Gag central domain reveals an ancient retroviral capsid
Structural highlights
FunctionGAG_FOAMV Involved in capsid formation and genome binding. Shortly after infection, interaction between incoming particle-associated Gag proteins and host dynein allows centrosomal targeting of the viral genome (associated to Gag), prior to nucleus translocation and integration into host genome.[1] [2] Publication Abstract from PubMedThe Spumaretrovirinae, or foamy viruses (FVs) are complex retroviruses that infect many species of monkey and ape. Despite little sequence homology, FV and orthoretroviral Gag proteins perform equivalent functions, including genome packaging, virion assembly, trafficking and membrane targeting. However, there is a paucity of structural information for FVs and it is unclear how disparate FV and orthoretroviral Gag molecules share the same function. To probe the functional overlap of FV and orthoretroviral Gag we have determined the structure of a central region of Gag from the Prototype FV (PFV). The structure comprises two all alpha-helical domains NtDCEN and CtDCEN that although they have no sequence similarity, we show they share the same core fold as the N- (NtDCA) and C-terminal domains (CtDCA) of archetypal orthoretroviral capsid protein (CA). Moreover, structural comparisons with orthoretroviral CA align PFV NtDCEN and CtDCEN with NtDCA and CtDCA respectively. Further in vitro and functional virological assays reveal that residues making inter-domain NtDCEN-CtDCEN interactions are required for PFV capsid assembly and that intact capsid is required for PFV reverse transcription. These data provide the first information that relates the Gag proteins of Spuma and Orthoretrovirinae and suggests a common ancestor for both lineages containing an ancient CA fold. Structure of a Spumaretrovirus Gag Central Domain Reveals an Ancient Retroviral Capsid.,Ball NJ, Nicastro G, Dutta M, Pollard DJ, Goldstone DC, Sanz-Ramos M, Ramos A, Mullers E, Stirnnagel K, Stanke N, Lindemann D, Stoye JP, Taylor WR, Rosenthal PB, Taylor IA PLoS Pathog. 2016 Nov 9;12(11):e1005981. doi: 10.1371/journal.ppat.1005981., eCollection 2016 Nov. PMID:27829070[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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