Abstract
The X-ray crystal structure of the complex of protein tyrosine phosphatase 1B with nitrate anion has been determined and modelled quantum-mechanically. Two protomers were present in the structure, one with the mechanistically important WPD loop closed and the other with this loop open. Nitrate was observed bound to each protomer, making close contacts with the S atom of the catalytic cysteine and a tyrosine residue from a crystallographically related protomer.
Keywords:
nitrate; protein tyrosine phosphatase 1B; transition-state mimics.
MeSH terms
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Biocatalysis
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Catalytic Domain
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Crystallography, X-Ray
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Escherichia coli / genetics
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Escherichia coli / metabolism
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Humans
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Ligands
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Models, Molecular
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Molecular Mimicry*
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Nitrates / chemistry*
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Nitrates / metabolism
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Promoter Regions, Genetic
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Protein Structure, Secondary
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Protein Structure, Tertiary
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Protein Tyrosine Phosphatase, Non-Receptor Type 1 / chemistry*
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Protein Tyrosine Phosphatase, Non-Receptor Type 1 / genetics
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Protein Tyrosine Phosphatase, Non-Receptor Type 1 / metabolism
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Quantum Theory
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Substrate Specificity
Substances
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Ligands
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Nitrates
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Recombinant Proteins
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PTPN1 protein, human
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Protein Tyrosine Phosphatase, Non-Receptor Type 1