5NCR
OH1 from the Orf virus: a tyrosine phosphatase that displays distinct structural features and triple substrate specificity
Summary for 5NCR
| Entry DOI | 10.2210/pdb5ncr/pdb |
| Descriptor | tyrosine phosphatase, PHOSPHATE ION, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | tyrosine-phosphatase, homodimer, disulfide bridge, phosphate binding site, hydrolase |
| Biological source | Orf virus (ORFV) |
| Total number of polymer chains | 2 |
| Total formula weight | 40702.90 |
| Authors | Segovia, D.,Haouz, A.,Berois, M.,Villarino, A.,Andre-Leroux, G. (deposition date: 2017-03-06, release date: 2017-08-09, Last modification date: 2024-01-17) |
| Primary citation | Segovia, D.,Haouz, A.,Porley, D.,Olivero, N.,Martinez, M.,Mariadassou, M.,Berois, M.,Andre-Leroux, G.,Villarino, A. OH1 from Orf Virus: A New Tyrosine Phosphatase that Displays Distinct Structural Features and Triple Substrate Specificity. J. Mol. Biol., 429:2816-2824, 2017 Cited by PubMed Abstract: 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 homolog 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. PubMed: 28754374DOI: 10.1016/j.jmb.2017.07.017 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.89 Å) |
Structure validation
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