View source for 5ncr


==OH1 from the Orf virus: a tyrosine phosphatase that displays distinct structural features and triple substrate specificity==
<StructureSection load='5ncr' size='340' side='right'caption='[[5ncr]], [[Resolution|resolution]] 1.89&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5ncr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Orf_virus Orf virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NCR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NCR FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.89&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=5ncr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ncr OCA], [https://pdbe.org/5ncr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ncr RCSB], [https://www.ebi.ac.uk/pdbsum/5ncr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ncr ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q6TW43_ORFV Q6TW43_ORFV] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Viral tyrosine phosphatases such as VH1 from Vaccinia and Variola virus are recognized as important effectors of host-pathogen interactions. While proteins sharing sequence to VH1 have been identified in other viruses, their structural and functional characterization is not known. In this work, we determined the crystal structure of the VH1 homologue in the Orf virus, herein named OH1. Similarly to Variola and Vaccinia VH1, the structure of OH1 shows a dimer with the typical dual specificity phosphatase fold. In contrast to VH1, the OH1 dimer is covalently stabilized by a disulfide bond involving residue Cys15 in the N-terminal helix alpha-1 of both monomers, and Cys15 is a conserved residue within the Parapoxvirus genus. The in vitro functional characterization confirms that OH1 is a dual specificity phosphatase, and reveals its ability to dephosphorylate phosphatidylinositol 3,5 bisphosphate, a new activity potentially relevant in phosphoinositide recycling during virion maturation.

OH1 from Orf virus: A new tyrosine phosphatase that displays distinct structural features and triple substrate specificity.,Segovia D, Haouz A, Porley D, Olivero N, Martinez M, Mariadassou M, Berois M, Andre-Leroux G, Villarino A J Mol Biol. 2017 Jul 25. pii: S0022-2836(17)30367-4. doi:, 10.1016/j.jmb.2017.07.017. PMID:28754374<ref>PMID:28754374</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5ncr" style="background-color:#fffaf0;"></div>

==See Also==
*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Orf virus]]
[[Category: Andre-Leroux G]]
[[Category: Berois M]]
[[Category: Haouz A]]
[[Category: Segovia D]]
[[Category: Villarino A]]