4xal

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Revision as of 14:25, 29 March 2017

Crystal structure of the conserved core domain of VP22 from HSV-1

Structural highlights

4xal is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[VP22_HHV11] Tegument protein that plays different roles during the time course of infection. Participates in both the accumulation of viral mRNAs and viral protein translation at late time of infection. Modulates the RNase activity of the virion host shutoff protein UL41 probably to ensure necessary levels of key cellular mRNAs and proteins. Plays a role in microtubule reorganization that occurs after viral infection by stabilizing microtubule network. Finally, may prevent nucleosomal deposition onto the viral genome by interacting with and inhibiting host SET.^[1] ^[2] ^[3] ^[4] ^[5] ^[6]

Publication Abstract from PubMed

The viral tegument is a layer of proteins between the herpesvirus capsid and its outer envelope. According to phylogenetic studies, only a third of these proteins are conserved amongst the three subfamilies (Alpha-, Beta- and Gammaherpesvirinae) of the family Herpesviridae. Although some of these tegument proteins have been studied in more detail, the structure and function of the majority of them are still poorly characterized. VP22 from Herpes simplex virus 1 (subfamily Alphaherpesvirinae) is a highly interacting tegument protein that has been associated with tegument assembly. We have determined the crystal structure of the conserved core domain of VP22, which reveals an elongated dimer with several potential protein-protein interaction regions and a peptide-binding site. The structure provides us with the structural basics to understand the numerous functional mutagenesis studies of VP22 found in the literature. It also establishes an unexpected structural homology to the tegument protein ORF52 from Murid herpesvirus 68 (subfamily Gammaherpesvirinae). Homologues for both VP22 and ORF52 have been identified in their respective subfamilies. Although there is no obvious sequence overlap in the two subfamilies, this structural conservation provides compelling structural evidence for shared ancestry and functional conservation.

VP22 core domain from Herpes simplex virus 1 reveals a surprising structural conservation in both the Alpha- and Gammaherpesvirinae subfamilies.,Hew K, Dahlroth SL, Pan LX, Cornvik T, Nordlund P J Gen Virol. 2015 Jun;96(Pt 6):1436-45. doi: 10.1099/vir.0.000078. Epub 2015 Feb , 24. PMID:26068188^[7]

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

References

↑ van Leeuwen H, Okuwaki M, Hong R, Chakravarti D, Nagata K, O'Hare P. Herpes simplex virus type 1 tegument protein VP22 interacts with TAF-I proteins and inhibits nucleosome assembly but not regulation of histone acetylation by INHAT. J Gen Virol. 2003 Sep;84(Pt 9):2501-10. PMID:12917472
↑ Yedowitz JC, Kotsakis A, Schlegel EF, Blaho JA. Nuclear localizations of the herpes simplex virus type 1 tegument proteins VP13/14, vhs, and VP16 precede VP22-dependent microtubule reorganization and VP22 nuclear import. J Virol. 2005 Apr;79(8):4730-43. PMID:15795259 doi:http://dx.doi.org/10.1128/JVI.79.8.4730-4743.2005
↑ Mbong EF, Woodley L, Dunkerley E, Schrimpf JE, Morrison LA, Duffy C. Deletion of the herpes simplex virus 1 UL49 gene results in mRNA and protein translation defects that are complemented by secondary mutations in UL41. J Virol. 2012 Nov;86(22):12351-61. doi: 10.1128/JVI.01975-12. Epub 2012 Sep 5. PMID:22951838 doi:http://dx.doi.org/10.1128/JVI.01975-12
↑ Maringer K, Stylianou J, Elliott G. A network of protein interactions around the herpes simplex virus tegument protein VP22. J Virol. 2012 Dec;86(23):12971-82. doi: 10.1128/JVI.01913-12. Epub 2012 Sep 19. PMID:22993164 doi:http://dx.doi.org/10.1128/JVI.01913-12
↑ Starkey JL, Han J, Chadha P, Marsh JA, Wills JW. Elucidation of the block to herpes simplex virus egress in the absence of tegument protein UL16 reveals a novel interaction with VP22. J Virol. 2014 Jan;88(1):110-9. doi: 10.1128/JVI.02555-13. Epub 2013 Oct 16. PMID:24131716 doi:http://dx.doi.org/10.1128/JVI.02555-13
↑ Elliott G, O'Hare P. Herpes simplex virus type 1 tegument protein VP22 induces the stabilization and hyperacetylation of microtubules. J Virol. 1998 Aug;72(8):6448-55. PMID:9658087
↑ Hew K, Dahlroth SL, Pan LX, Cornvik T, Nordlund P. VP22 core domain from Herpes simplex virus 1 reveals a surprising structural conservation in both the Alpha- and Gammaherpesvirinae subfamilies. J Gen Virol. 2015 Jun;96(Pt 6):1436-45. doi: 10.1099/vir.0.000078. Epub 2015 Feb , 24. PMID:26068188 doi:http://dx.doi.org/10.1099/vir.0.000078

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4xal"

Categories: Dahlroth, S L | Hew, K | Nordlund, P | Hsv-1 | Mhv-68 | Orf52 | Viral protein | Vp22

@@ Line 1: / Line 1: @@
 ==Crystal structure of the conserved core domain of VP22 from HSV-1==
 <StructureSection load='4xal' size='340' side='right' caption='[[4xal]], [[Resolution|resolution]] 1.87&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[4xal]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XAL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XAL 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=4xal FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xal OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4xal RCSB], [http://www.ebi.ac.uk/pdbsum/4xal PDBsum]</span></td></tr>
+</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=4xal FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xal OCA], [http://pdbe.org/4xal PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xal RCSB], [http://www.ebi.ac.uk/pdbsum/4xal PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xal ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 15: / Line 16: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4xal" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4xal

From Proteopedia

Revision as of 14:25, 29 March 2017

Crystal structure of the conserved core domain of VP22 from HSV-1

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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