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PDBsum entry 2esb

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Hydrolase PDB id
2esb
Jmol
Contents
Protein chain
162 a.a.
Ligands
ACT
EPE
Waters ×169

References listed in PDB file
Key reference
Title Structure of human dsp18, A member of the dual-Specificity protein tyrosine phosphatase family
Authors D.G.Jeong, Y.H.Cho, T.S.Yoon, J.H.Kim, J.H.Son, S.E.Ryu, S.J.Kim.
Ref. ACTA CRYSTALLOGR.,SECT.D, 2006, 62, 582-588. [DOI no: 10.1107/S0907444906010109]
PubMed id 16699184
Abstract
The human dual-specificity protein phosphatase 18 (DSP18) gene and its protein product have recently been characterized. Like most DSPs, DSP18 displays dephosphorylating activity towards both phosphotyrosine and phosphothreonine residues. However, DSP18 is distinct from other known DSPs in terms of the existence of approximately 30 residues at the C-terminus of the catalytic domain and an unusual optimum activity profile at 328 K. The crystal structure of human DSP18 has been determined at 2.0 A resolution. The catalytic domain of DSP18 adopts a fold similar to that known for other DSP structures. Although good alignments are found with other DSPs, substantial differences are also found in the regions surrounding the active site, suggesting that DSP18 constitutes a unique structure with a distinct substrate specificity. Furthermore, the residues at the C-terminus fold into two antiparallel beta-strands and participate in extensive interactions with the catalytic domain, explaining the thermostability of DSP18.
Figure 3.
Figure 3 Active site. (a) The difference electron-density map for DSP18 was generated with the final model, omitting the bound HEPES. The stereo map contoured at the 3.0 level was presented as superposed with the refined model. The hydrogen-bonding interactions around the active site are represented by dashed lines. (b) Electrostatic potential surfaces of DSP18 and VHR (PDB code [183]1vhr ) are presented. Positive and negative potentials are coloured blue and red, respectively. Residues near the active site are labelled.
Figure 4.
Figure 4 CT motif. (a) The hydrophobic interactions between the catalytic domain and the CT motif. The side chains of residues involved in the hydrophobic interactions are represented and labelled. Residues in the catalytic domain are coloured grey, whereas those in the CT motif are coloured red. (b) Difference F[o] - F[c] electron-density map around the CT motif omitted for map calculation drawn in stereo with the refined model. The map was contoured at a level of 3.0 . Residues with atoms that participate in crystal contacts with neighbours are coloured cyan.
The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2006, 62, 582-588) copyright 2006.
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