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3cm3

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Revision as of 21:53, 9 February 2016

High Resolution Crystal Structure of the Vaccinia Virus Dual-Specificity Phosphatase VH1

Structural highlights

3cm3 is a 1 chain structure with sequence from Vaccinia virus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	2rf6, 3ceo
Gene:	H1 ORF (Vaccinia virus)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[DUSP_VACCW] Serine/Tyrosine phosphatase which down-regulates cellular antiviral response by dephosphorylating activated host STAT1 and blocking interferon (IFN)-stimulated innate immune responses. Dephosphorylates the A17 protein.^[1] ^[2] ^[3] ^[4] ^[5]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The Vaccinia virus H1 gene product, VH1, is a dual specificity phosphatase that down-regulates the cellular antiviral response by dephosphorylating STAT1. The crystal structure of VH1, determined at 1.32 A resolution, reveals a novel dimeric quaternary structure, which exposes two active sites spaced approximately 39 A away from each other. VH1 forms a stable dimer via an extensive domain swap of the N-terminal helix (residues 1-20). In vitro, VH1 can dephosphorylate activated STAT1, in a reaction that is competed by the nuclear transport adapter importin alpha5. Interestingly, VH1 is inactive with respect to STAT1 bound to DNA, suggesting that the viral phosphatase acts predominantly on the cytoplasmic pool of activated STAT1. We propose that the dimeric quaternary structure of VH1 is essential for specific recognition of activated STAT1, which prevents its nuclear translocation, thus blocking interferon-gamma signal transduction and antiviral response.

Dimeric quaternary structure of the prototypical dual specificity phosphatase VH1.,Koksal AC, Nardozzi JD, Cingolani G J Biol Chem. 2009 Apr 10;284(15):10129-37. Epub 2009 Feb 10. PMID:19211553^[6]

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

References

↑ Derrien M, Punjabi A, Khanna M, Grubisha O, Traktman P. Tyrosine phosphorylation of A17 during vaccinia virus infection: involvement of the H1 phosphatase and the F10 kinase. J Virol. 1999 Sep;73(9):7287-96. PMID:10438817
↑ Najarro P, Traktman P, Lewis JA. Vaccinia virus blocks gamma interferon signal transduction: viral VH1 phosphatase reverses Stat1 activation. J Virol. 2001 Apr;75(7):3185-96. PMID:11238845 doi:http://dx.doi.org/10.1128/JVI.75.7.3185-3196.2001
↑ Guan KL, Broyles SS, Dixon JE. A Tyr/Ser protein phosphatase encoded by vaccinia virus. Nature. 1991 Mar 28;350(6316):359-62. PMID:1848923 doi:http://dx.doi.org/10.1038/350359a0
↑ Mann BA, Huang JH, Li P, Chang HC, Slee RB, O'Sullivan A, Anita M, Yeh N, Klemsz MJ, Brutkiewicz RR, Blum JS, Kaplan MH. Vaccinia virus blocks Stat1-dependent and Stat1-independent gene expression induced by type I and type II interferons. J Interferon Cytokine Res. 2008 Jun;28(6):367-80. doi: 10.1089/jir.2007.0113. PMID:18593332 doi:http://dx.doi.org/10.1089/jir.2007.0113
↑ Koksal AC, Cingolani G. Dimerization of Vaccinia virus VH1 is essential for dephosphorylation of STAT1 at tyrosine 701. J Biol Chem. 2011 Apr 22;286(16):14373-82. doi: 10.1074/jbc.M111.226357. Epub, 2011 Mar 1. PMID:21362620 doi:http://dx.doi.org/10.1074/jbc.M111.226357
↑ Koksal AC, Nardozzi JD, Cingolani G. Dimeric quaternary structure of the prototypical dual specificity phosphatase VH1. J Biol Chem. 2009 Apr 10;284(15):10129-37. Epub 2009 Feb 10. PMID:19211553 doi:10.1074/jbc.M808362200

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3cm3"

@@ Line 6: / Line 6: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2rf6|2rf6]], [[3ceo|3ceo]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">H1 ORF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10245 Vaccinia virus])</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=3cm3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cm3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3cm3 RCSB], [http://www.ebi.ac.uk/pdbsum/3cm3 PDBsum]</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=3cm3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cm3 OCA], [http://pdbe.org/3cm3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3cm3 RCSB], [http://www.ebi.ac.uk/pdbsum/3cm3 PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/DUSP_VACCV DUSP_VACCV]] Serine/Tyrosine phosphatase which down-regulates cellular antiviral response by dephosphorylating activated host STAT1 and blocking interferon (IFN)-stimulated innate immune responses. Dephosphorylates the A17 protein.<ref>PMID:1848923</ref> <ref>PMID:10438817</ref> <ref>PMID:11238845</ref> <ref>PMID:18593332</ref> <ref>PMID:21362620</ref>
+[[http://www.uniprot.org/uniprot/DUSP_VACCW DUSP_VACCW]] Serine/Tyrosine phosphatase which down-regulates cellular antiviral response by dephosphorylating activated host STAT1 and blocking interferon (IFN)-stimulated innate immune responses. Dephosphorylates the A17 protein.<ref>PMID:10438817</ref> <ref>PMID:11238845</ref> <ref>PMID:1848923</ref> <ref>PMID:18593332</ref> <ref>PMID:21362620</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 18: / Line 18: @@
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3cm3 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 28: / Line 28: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3cm3" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

3cm3

From Proteopedia

Revision as of 21:53, 9 February 2016

High Resolution Crystal Structure of the Vaccinia Virus Dual-Specificity Phosphatase VH1

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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