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PDBsum entry 1qz0
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Hydrolase/hydrolase inhibitor
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PDB id
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1qz0
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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High-Resolution structure of the yersinia pestis protein tyrosine phosphatase yoph in complex with a phosphotyrosyl mimetic-Containing hexapeptide.
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Authors
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J.Phan,
K.Lee,
S.Cherry,
J.E.Tropea,
T.R.Burke,
D.S.Waugh.
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Ref.
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Biochemistry, 2003,
42,
13113-13121.
[DOI no: ]
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PubMed id
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Abstract
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Yersinia pestis, the causative agent of bubonic plague, secretes a
eukaryotic-like protein tyrosine phosphatase (PTPase) termed Yersinia outer
protein H (YopH) that is essential for virulence. We have determined, for the
first time, the crystal structure of the YopH PTPase domain in complex with a
nonhydrolyzable substrate analogue, the hexapeptide mimetic
Ac-DADE-F(2)Pmp-L-NH(2). As anticipated, the mode of ligand binding in the
active site is similar to the way in which the corresponding phosphohexapeptide
binds to the structurally homologous human PTP1B. Unexpectedly, however, the
crystal structure also revealed a second substrate-binding site in YopH that is
not present in PTP1B. The mode of binding and structural conformation of the
hexapeptide analogue is quite different in the two sites. Although the
biological function of the second substrate-binding site remains to be
investigated, the structure of a substrate analogue in the active site of Y.
pestis YopH opens the door for the structure-based design and optimization of
therapeutic countermeasures to combat this potential agent of bioterrorism.
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