1wrm

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Revision as of 17:47, 12 November 2007

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spinqualitylabelsall models 1wrm, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of JSP-1

Overview

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.

About this Structure

1WRM is a Single protein structure of sequence from Homo sapiens with MES as ligand. Active as Protein-tyrosine-phosphatase, with EC number 3.1.3.48 Full crystallographic information is available from OCA.

Reference

Crystal structure of human dual specificity phosphatase, JNK stimulatory phosphatase-1, at 1.5 A resolution., Yokota T, Nara Y, Kashima A, Matsubara K, Misawa S, Kato R, Sugio S, Proteins. 2007 Feb 1;66(2):272-8. PMID:17068812

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