6t64

From Proteopedia

(Difference between revisions)

Current revision

A model of the EIAV CA-SP hexamer (C6) from Gag-deltaMA spheres assembled at pH6

6t64, resolution 3.70Å

Structural highlights

6t64 is a 3 chain structure with sequence from Equine infectious anemia virus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 3.7Å
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GAG_EIAV9 Matrix protein p15 forms the outer shell of the core of the virus, lining the inner surface of the viral membrane. Capsid protein p26 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex. Nucleocapsid protein p11 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers (By similarity). p9 plays a role in budding of the assembled particle by interacting with PDCD6IP/AIP1.

Publication Abstract from PubMed

Retrovirus assembly is driven by the multidomain structural protein Gag. Interactions between the capsid domains (CA) of Gag result in Gag multimerization, leading to an immature virus particle that is formed by a protein lattice based on dimeric, trimeric, and hexameric protein contacts. Among retroviruses the inter- and intra-hexamer contacts differ, especially in the N-terminal sub-domain of CA (CANTD). For HIV-1 the cellular molecule inositol hexakisphosphate (IP6) interacts with and stabilizes the immature hexamer, and is required for production of infectious virus particles. We have used in vitro assembly, cryo-electron tomography and subtomogram averaging, atomistic molecular dynamics simulations and mutational analyses to study the HIV-related lentivirus equine infectious anemia virus (EIAV). In particular, we sought to understand the structural conservation of the immature lentivirus lattice and the role of IP6 in EIAV assembly. Similar to HIV-1, IP6 strongly promoted in vitro assembly of EIAV Gag proteins into virus-like particles (VLPs), which took three morphologically highly distinct forms: narrow tubes, wide tubes, and spheres. Structural characterization of these VLPs to sub-4A resolution unexpectedly showed that all three morphologies are based on an immature lattice with preserved key structural components, highlighting the structural versatility of CA to form immature assemblies. A direct comparison between EIAV and HIV revealed that both lentiviruses maintain similar immature interfaces, which are established by both conserved and non-conserved residues. In both EIAV and HIV-1, IP6 regulates immature assembly via conserved lysine residues within the CACTD and SP. Lastly, we demonstrate that IP6 stimulates in vitro assembly of immature particles of several other retroviruses in the lentivirus genus, suggesting a conserved role for IP6 in lentiviral assembly.

Structures of immature EIAV Gag lattices reveal a conserved role for IP6 in lentivirus assembly.,Dick RA, Xu C, Morado DR, Kravchuk V, Ricana CL, Lyddon TD, Broad AM, Feathers JR, Johnson MC, Vogt VM, Perilla JR, Briggs JAG, Schur FKM PLoS Pathog. 2020 Jan 27;16(1):e1008277. doi: 10.1371/journal.ppat.1008277., eCollection 2020 Jan. PMID:31986188^[1]

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

References

↑ Dick RA, Xu C, Morado DR, Kravchuk V, Ricana CL, Lyddon TD, Broad AM, Feathers JR, Johnson MC, Vogt VM, Perilla JR, Briggs JAG, Schur FKM. Structures of immature EIAV Gag lattices reveal a conserved role for IP6 in lentivirus assembly. PLoS Pathog. 2020 Jan 27;16(1):e1008277. doi: 10.1371/journal.ppat.1008277., eCollection 2020 Jan. PMID:31986188 doi:http://dx.doi.org/10.1371/journal.ppat.1008277

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/6t64"

@@ Line 3: / Line 3: @@
 <SX load='6t64' size='340' side='right' viewer='molstar' caption='[[6t64]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6t64]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Eiav Eiav]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T64 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6T64 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6t64]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Equine_infectious_anemia_virus Equine infectious anemia virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T64 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6T64 FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gag ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11665 EIAV])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.7&#8491;</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=6t64 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t64 OCA], [https://pdbe.org/6t64 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6t64 RCSB], [https://www.ebi.ac.uk/pdbsum/6t64 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6t64 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/GAG_EIAV9 GAG_EIAV9]] Matrix protein p15 forms the outer shell of the core of the virus, lining the inner surface of the viral membrane.  Capsid protein p26 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex.  Nucleocapsid protein p11 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers (By similarity).  p9 plays a role in budding of the assembled particle by interacting with PDCD6IP/AIP1.
+[https://www.uniprot.org/uniprot/GAG_EIAV9 GAG_EIAV9] Matrix protein p15 forms the outer shell of the core of the virus, lining the inner surface of the viral membrane.  Capsid protein p26 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex.  Nucleocapsid protein p11 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers (By similarity).  p9 plays a role in budding of the assembled particle by interacting with PDCD6IP/AIP1.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 25: / Line 25: @@
 __TOC__
 </SX>
-[[Category: Eiav]]
-[[Category: Large Structures]]
-[[Category: Briggs, J A.G]]
-[[Category: Broad, A M]]
-[[Category: Dick, R A]]
-[[Category: Feathers, J R]]
-[[Category: Johnson, M C]]
-[[Category: Kravchuk, V]]
-[[Category: Lyddon, T D]]
-[[Category: Morado, D R]]
-[[Category: Perilla, J R]]
-[[Category: Ricana, C L]]
-[[Category: Schur, F K.M]]
-[[Category: Vogt, V M]]
-[[Category: Xu, C]]
-[[Category: Capsid]]
 [[Category: Equine infectious anemia virus]]
-[[Category: Gag]]
+[[Category: Large Structures]]
-[[Category: Inositolhexakiphosphate]]
+[[Category: Briggs JAG]]
-[[Category: Ip6]]
+[[Category: Broad AM]]
-[[Category: Lentivirus]]
+[[Category: Dick RA]]
-[[Category: Phytic acid]]
+[[Category: Feathers JR]]
-[[Category: Retrovirus]]
+[[Category: Johnson MC]]
-[[Category: Viral protein]]
+[[Category: Kravchuk V]]
+[[Category: Lyddon TD]]
+[[Category: Morado DR]]
+[[Category: Perilla JR]]
+[[Category: Ricana CL]]
+[[Category: Schur FKM]]
+[[Category: Vogt VM]]
+[[Category: Xu C]]

6t64

From Proteopedia

Current revision

A model of the EIAV CA-SP hexamer (C6) from Gag-deltaMA spheres assembled at pH6

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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