1WRM

Crystal structure of JSP-1

Summary for 1WRM

• Entry DOI: 10.2210/pdb1wrm/pdb
• Descriptor: dual specificity phosphatase 22, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID (3 entities in total)
• Functional Keywords: phosphatase, dsp, jnk, hydrolase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm (By similarity): Q9NRW4
• Total number of polymer chains: 1
• Total formula weight: 18876.50

Authors

Yokota, T.,Kashima, A.,Kato, R.,Sugio, S. (deposition date: 2004-10-22, release date: 2005-10-22, Last modification date: 2024-03-13)

Primary citation

Yokota, T.,Nara, Y.,Kashima, A.,Matsubara, K.,Misawa, S.,Kato, R.,Sugio, S.
Crystal structure of human dual specificity phosphatase, JNK stimulatory phosphatase-1, at 1.5 A resolution
Proteins, 66:272-278, 2006

PubMed Abstract: Human JNK stimulatory phosphatase-1 (JSP-1) is a novel member of dual specificity phosphatases. A C-terminus truncated JSP-1 was expressed in Escherichia coli and was crystallized using the sitting-drop vapor diffusion method. Thin-plate crystals obtained at 278 K belong to a monoclinic space group, C2, with unit-cell parameters a = 84.0 A, b = 49.3 A, c = 47.3 A, and beta = 119.5 degrees , and diffract up to 1.5 A resolution at 100 K. The structure of JSP-1 has a single compact (alpha/beta) domain, which consists of six alpha-helices and five beta-strands, and shows a conserved structural scaffold in regard to both DSPs and PTPs. A cleft formed by a PTP-loop at the active site is very shallow, and is occupied by one sulfonate compound, MES, at the bottom. In the binary complex structure of JSP-1 with MES, the conformations of three important segments in regard to the catalytic mechanism are not similar to those in PTP1B. JSP-1 has no loop corresponding to the Lys120-loop of PTP1B, and tryptophan residue corresponding to the substrate-stacking in PTP1B is substituted by alanine residue in JSP-1.

PubMed: 17068812
DOI: 10.1002/prot.21152

Experimental method

X-RAY DIFFRACTION (1.5 Å)