2YDU
Crystal structure of YopH in complex with 3-(1,1-dioxido-3- oxoisothiazolidin-5-yl)benzaldeyde
Summary for 2YDU
| Entry DOI | 10.2210/pdb2ydu/pdb |
| Related | 1QZ0 2Y2F |
| Descriptor | OUTER PROTEIN H PHOSPHATASE, 3-[(2S)-1,1-DIOXIDO-4-OXOTETRAHYDROTHIOPHEN-2-YL]BENZALDEHYDE (3 entities in total) |
| Functional Keywords | hydrolase, antiplague drug design |
| Biological source | YERSINIA PESTIS |
| Total number of polymer chains | 1 |
| Total formula weight | 33792.14 |
| Authors | Lountos, G.T.,Kim, S.E.,Bahta, M.,Ulrich, R.G.,Waugh, D.S.,Burke, T.R. (deposition date: 2011-03-24, release date: 2011-11-02, Last modification date: 2023-12-20) |
| Primary citation | Kim, S.E.,Bahta, M.,Lountos, G.T.,Ulrich, R.G.,Burke, T.R.,Waugh, D.S. Isothiazolidinone (Izd) as a Phosphoryl Mimetic in Inhibitors of the Yersinia Pestis Protein Tyrosine Phosphatase Yoph. Acta Crystallogr.,Sect.D, 67:639-, 2011 Cited by PubMed Abstract: Isothiazolidinone (IZD) heterocycles can act as effective components of protein tyrosine phosphatase (PTP) inhibitors by simultaneously replicating the binding interactions of both a phosphoryl group and a highly conserved water molecule, as exemplified by the structures of several PTP1B-inhibitor complexes. In the first unambiguous demonstration of IZD interactions with a PTP other than PTP1B, it is shown by X-ray crystallography that the IZD motif binds within the catalytic site of the Yersinia pestis PTP YopH by similarly displacing a highly conserved water molecule. It is also shown that IZD-based bidentate ligands can inhibit YopH in a nonpromiscuous fashion at low micromolar concentrations. Hence, the IZD moiety may represent a useful starting point for the development of YopH inhibitors. PubMed: 21697602DOI: 10.1107/S0907444911018610 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.79 Å) |
Structure validation
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