title: Crystal structure of human dual specificity phosphatase, JNK stimulatory phosphatase-1, at 1.5 A resolution.
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.
authors.affiliation: ZOEGENE Corporation, 1000 Kamoshida, Aoba, Yokohama, Kanagawa 227-8502, Japan.
authors.forename: Takehiro
authors.initials: T
authors.lastname: Yokota
authors.forename: Yukinori
authors.initials: Y
authors.lastname: Nara
authors.forename: Akiko
authors.initials: A
authors.lastname: Kashima
authors.forename: Keiko
authors.initials: K
authors.lastname: Matsubara
authors.forename: Satoru
authors.initials: S
authors.lastname: Misawa
authors.forename: Ryohei
authors.initials: R
authors.lastname: Kato
authors.forename: Shigetoshi
authors.initials: S
authors.lastname: Sugio
mesh_terms: D017738:Alkanesulfonic Acids / Q000378:metabolism; D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002384:Catalysis; D018360:Crystallography, X-Ray; D054637:Dual-Specificity Phosphatases; D006801:Humans; D051379:Mice; D054639:Mitogen-Activated Protein Kinase Phosphatases; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009025:Morpholines / Q000378:metabolism; D010749:Phosphoprotein Phosphatases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D010766:Phosphorylation; D011485:Protein Binding; D011487:Protein Conformation; D054645:Protein Phosphatase 1; D011499:Protein Processing, Post-Translational; D017433:Protein Structure, Secondary; D054562:Protein Tyrosine Phosphatase, Non-Receptor Type 1; D017027:Protein Tyrosine Phosphatases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000302:isolation & purification; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
chemical_list: D017738:Alkanesulfonic Acids; D009025:Morpholines; D011993:Recombinant Fusion Proteins; C004550:2-(N-morpholino)ethanesulfonic acid; D054639:Mitogen-Activated Protein Kinase Phosphatases; D010749:Phosphoprotein Phosphatases; D054645:Protein Phosphatase 1; C442824:DUSP22 protein, human; D054637:Dual-Specificity Phosphatases; C522152:Dusp22 protein, mouse; C516607:PTPN1 protein, human; D054562:Protein Tyrosine Phosphatase, Non-Receptor Type 1; D017027:Protein Tyrosine Phosphatases; C516609:Ptpn1 protein, mouse