2GWO

crystal structure of TMDP

Summary for 2GWO

• Entry DOI: 10.2210/pdb2gwo/pdb
• Descriptor: Dual specificity protein phosphatase 13 (2 entities in total)
• Functional Keywords: alpha/beta, hydrolase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 4
• Total formula weight: 88698.38

Authors

Kim, S.J.,Ryu, S.E.,Kim, J.H. (deposition date: 2006-05-05, release date: 2007-03-20, Last modification date: 2024-03-13)

Primary citation

Kim, S.J.,Jeong, D.G.,Yoon, T.S.,Son, J.H.,Cho, S.K.,Ryu, S.E.,Kim, J.H.
Crystal structure of human TMDP, a testis-specific dual specificity protein phosphatase: implications for substrate specificity
Proteins, 66:239-245, 2007

PubMed Abstract: The testis- and skeletal-muscle-specific dual-specificity phosphatase (TMDP) is a member of the dual-specificity phosphatase (DSP) subgroup of protein tyrosine phosphatases. TMDP has similar activities toward both tyrosine and threonine phosphorylated substrates, and is supposed to be involved in spermatogenesis. Here, we report the crystal structure of human TMDP at a resolution of 2.4 A. In spite of high sequence similarity with other DSPs, the crystal structure of TMDP shows distinct structural motifs and surface properties. In TMDP, the alpha1-beta1 loop, a substrate recognition motif is located further away from the active site loop in comparison to prototype DSP Vaccinia H1 related phophatase (VHR), which preferentially dephosphorylates tyrosine phosphorylated substrates and down-regulates MAP kinase signaling. Residues in the active site residues of TMDP are smaller in size and more hydrophobic than those of VHR. In addition, TMDP cannot be aligned with VHR in loop beta3-alpha4. These differences in the active site of TMDP result in a flat and wide pocket structure, allowing equal binding of phosphotyrosine and phosphothreonine substrates.

PubMed: 17044055
DOI: 10.1002/prot.21197

Experimental method

X-RAY DIFFRACTION (2.4 Å)