3M4U
Crystal Structure of Trypanosoma brucei Protein Tyrosine Phosphatase TbPTP1
Summary for 3M4U
| Entry DOI | 10.2210/pdb3m4u/pdb |
| Descriptor | Tyrosine specific protein phosphatase, putative, PHOSPHATE ION (3 entities in total) |
| Functional Keywords | protein tyrosine phosphatase, hydrolase, protein phosphatase |
| Biological source | Trypanosoma brucei |
| Total number of polymer chains | 2 |
| Total formula weight | 68536.43 |
| Authors | Chou, S.,Alber, T.,Grundner, C. (deposition date: 2010-03-12, release date: 2010-05-05, Last modification date: 2024-02-21) |
| Primary citation | Chou, S.,Jensen, B.C.,Parsons, M.,Alber, T.,Grundner, C. The Trypanosoma brucei life cycle switch TbPTP1 is structurally conserved and dephosphorylates the nucleolar protein NOPP44/46. J.Biol.Chem., 285:22075-22081, 2010 Cited by PubMed Abstract: Trypanosoma brucei adapts to changing environments as it cycles through arrested and proliferating stages in the human and tsetse fly hosts. Changes in protein tyrosine phosphorylation of several proteins, including NOPP44/46, accompany T. brucei development. Moreover, inactivation of T. brucei protein-tyrosine phosphatase 1 (TbPTP1) triggers differentiation of bloodstream stumpy forms into tsetse procyclic forms through unknown downstream effects. Here, we link these events by showing that NOPP44/46 is a major substrate of TbPTP1. TbPTP1 substrate-trapping mutants selectively enrich NOPP44/46 from procyclic stage cell lysates, and TbPTP1 efficiently and selectively dephosphorylates NOPP44/46 in vitro. To provide insights into the mechanism of NOPP44/46 recognition, we determined the crystal structure of TbPTP1. The TbPTP1 structure, the first of a kinetoplastid protein-tyrosine phosphatase (PTP), emphasizes the conservation of the PTP fold, extending to one of the most diverged eukaryotes. The structure reveals surfaces that may mediate substrate specificity and affords a template for the design of selective inhibitors to interfere with T. brucei transmission. PubMed: 20444707DOI: 10.1074/jbc.M110.108860 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.392 Å) |
Structure validation
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