3I80
Protein Tyrosine Phosphatase 1B - Transition state analog for the second catalytic step
Summary for 3I80
| Entry DOI | 10.2210/pdb3i80/pdb |
| Related | 1A5Y 1PTU 2CM2 2HNQ 3I7Z |
| Descriptor | Tyrosine-protein phosphatase non-receptor type 1, VANADATE ION, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (5 entities in total) |
| Functional Keywords | hydrolase, p-loop, wpd-loop, protein phosphatase, vanadate, acetylation, endoplasmic reticulum, membrane, oxidation, phosphoprotein, polymorphism |
| Biological source | Homo sapiens (human) |
| Cellular location | Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side: P18031 |
| Total number of polymer chains | 1 |
| Total formula weight | 37879.00 |
| Authors | Brandao, T.A.S.,Johnson, S.J.,Hengge, A.C. (deposition date: 2009-07-09, release date: 2010-03-16, Last modification date: 2023-09-06) |
| Primary citation | Brandao, T.A.,Hengge, A.C.,Johnson, S.J. Insights into the reaction of protein-tyrosine phosphatase 1B: crystal structures for transition state analogs of both catalytic steps. J.Biol.Chem., 285:15874-15883, 2010 Cited by PubMed Abstract: Catalysis by protein-tyrosine phosphatase 1B (PTP1B) occurs through a two-step mechanism involving a phosphocysteine intermediate. We have solved crystal structures for the transition state analogs for both steps. Together with previously reported crystal structures of apo-PTP1B, the Michaelis complex of an inactive mutant, the phosphoenzyme intermediate, and the product complex, a full picture of all catalytic steps can now be depicted. The transition state analog for the first catalytic step comprises a ternary complex between the catalytic cysteine of PTP1B, vanadate, and the peptide DADEYL, a fragment of a physiological substrate. The equatorial vanadate oxygen atoms bind to the P-loop, and the apical positions are occupied by the peptide tyrosine oxygen and by the PTP1B cysteine sulfur atom. The vanadate assumes a trigonal bipyramidal geometry in both transition state analog structures, with very similar apical O-O distances, denoting similar transition states for both phosphoryl transfer steps. Detailed interactions between the flanking peptide and the enzyme are discussed. PubMed: 20236928DOI: 10.1074/jbc.M109.066951 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.25 Å) |
Structure validation
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