1ZZW

Crystal Structure of catalytic domain of Human MAP Kinase Phosphatase 5

Summary for 1ZZW

• Entry DOI: 10.2210/pdb1zzw/pdb
• Descriptor: Dual specificity protein phosphatase 10, SULFATE ION, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: phosphatase, mkp, ptp, hydrolase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: Q9Y6W6
• Total number of polymer chains: 2
• Total formula weight: 34589.57

Authors

Jeong, D.G.,Yoon, T.S.,Kim, J.H.,Shim, M.Y.,Jeong, S.K.,Son, J.H.,Ryu, S.E.,Kim, S.J. (deposition date: 2005-06-14, release date: 2006-07-04, Last modification date: 2024-03-13)

Primary citation

Jeong, D.G.,Yoon, T.S.,Kim, J.H.,Shim, M.Y.,Jeong, S.K.,Son, J.H.,Ryu, S.E.,Kim, S.J.
Crystal Structure of the Catalytic Domain of Human MAP Kinase Phosphatase 5: Structural Insight into Constitutively Active Phosphatase.
J.Mol.Biol., 360:946-955, 2006

PubMed Abstract: MAP kinase phosphatase 5 (MKP5) is a member of the mitogen-activated protein kinase phosphatase (MKP) family and selectively dephosphorylates JNK and p38. We have determined the crystal structure of the catalytic domain of human MKP5 (MKP5-C) to 1.6 A. In previously reported MKP-C structures, the residues that constitute the active site are seriously deviated from the active conformation of protein tyrosine phosphatases (PTPs), which are accompanied by low catalytic activity. High activities of MKPs are achieved by binding their cognate substrates, representing substrate-induced activation. However, the MKP5-C structure adopts an active conformation of PTP even in the absence of its substrate binding, which is consistent with the previous results that MKP5 solely possesses the intrinsic activity. Further, we identify a sequence motif common to the members of MKPs having low catalytic activity by comparing structures and sequences of other MKPs. Our structural information provides an explanation of constitutive activity of MKP5 as well as the structural insight into substrate-induced activation occurred in other MKPs.

PubMed: 16806267
DOI: 10.1016/j.jmb.2006.05.059

Experimental method

X-RAY DIFFRACTION (1.6 Å)