3CM3
High Resolution Crystal Structure of the Vaccinia Virus Dual-Specificity Phosphatase VH1
Summary for 3CM3
| Entry DOI | 10.2210/pdb3cm3/pdb |
| Related | 2RF6 3CEO |
| Descriptor | Dual specificity protein phosphatase, PHOSPHATE ION, BETA-MERCAPTOETHANOL, ... (4 entities in total) |
| Functional Keywords | dual-specificity phosphatase, vaccinia virus, vh1, hydrolase, late protein, protein phosphatase |
| Biological source | Vaccinia virus |
| Total number of polymer chains | 1 |
| Total formula weight | 20513.69 |
| Authors | Koksal, A.C.,Cingolani, G. (deposition date: 2008-03-20, release date: 2009-02-10, Last modification date: 2023-08-30) |
| Primary citation | Koksal, A.C.,Nardozzi, J.D.,Cingolani, G. Dimeric Quaternary Structure of the Prototypical Dual Specificity Phosphatase VH1. J.Biol.Chem., 284:10129-10137, 2009 Cited by PubMed Abstract: 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. PubMed: 19211553DOI: 10.1074/jbc.M808362200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.32 Å) |
Structure validation
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