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5m1h

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Structure of a Spumaretrovirus Gag central domain reveals an ancient retroviral capsid

Structural highlights

5m1h is a 1 chain structure with sequence from Human spumaretrovirus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[1] ^[2]

Publication Abstract from PubMed

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^[3]

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

References

↑ Cartellieri M, Herchenroder O, Rudolph W, Heinkelein M, Lindemann D, Zentgraf H, Rethwilm A. N-terminal Gag domain required for foamy virus particle assembly and export. J Virol. 2005 Oct;79(19):12464-76. PMID:16160174 doi:79/19/12464
↑ Petit C, Giron ML, Tobaly-Tapiero J, Bittoun P, Real E, Jacob Y, Tordo N, De The H, Saib A. Targeting of incoming retroviral Gag to the centrosome involves a direct interaction with the dynein light chain 8. J Cell Sci. 2003 Aug 15;116(Pt 16):3433-42. PMID:12857789 doi:http://dx.doi.org/10.1242/jcs.00613
↑ 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. Structure of a Spumaretrovirus Gag Central Domain Reveals an Ancient Retroviral Capsid. PLoS Pathog. 2016 Nov 9;12(11):e1005981. doi: 10.1371/journal.ppat.1005981., eCollection 2016 Nov. PMID:27829070 doi:http://dx.doi.org/10.1371/journal.ppat.1005981

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5m1h"

Categories: Human spumaretrovirus | Large Structures | Ball N | Nicastro G | Taylor IA

@@ Line 1: / Line 1: @@
 ==Structure of a Spumaretrovirus Gag central domain reveals an ancient retroviral capsid==
-<StructureSection load='5m1h' size='340' side='right' caption='[[5m1h]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='5m1h' size='340' side='right'caption='[[5m1h]]' scene=''>
 == 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5M1H FirstGlance]. <br>
+<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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5m1h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m1h OCA], [http://pdbe.org/5m1h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5m1h RCSB], [http://www.ebi.ac.uk/pdbsum/5m1h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5m1h ProSAT]</span></td></tr>
+</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>
 == Function ==
-[[http://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>
+[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;">
 == Publication Abstract from PubMed ==
@@ Line 17: / Line 18: @@
 </div>
 <div class="pdbe-citations 5m1h" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Gag polyprotein 3D structures|Gag polyprotein 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Ball, N]]
+[[Category: Human spumaretrovirus]]
-[[Category: Nicastro, G]]
+[[Category: Large Structures]]
-[[Category: Taylor, I A]]
+[[Category: Ball N]]
-[[Category: Foamy virus]]
+[[Category: Nicastro G]]
-[[Category: Gag]]
+[[Category: Taylor IA]]
-[[Category: Viral protein]]

5m1h

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Current revision

Structure of a Spumaretrovirus Gag central domain reveals an ancient retroviral capsid

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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