Structure of a human lysosomal sulfatase

Structure

Volumn 5, Issue 2, 1997, Pages 277-289

  Bond, Charles S ^a   Clements, Peter R ^b   Ashby, Samantha J ^a   Collyer, Charles A ^a   Harrop, Stephen J ^a   Hopwood, John J ^b   Guss, J Mitchell ^a  

^a UNIVERSITY OF SYDNEY   (Australia)

^b WOMEN S AND CHILDREN S HOSPITAL   (Australia)

Author keywords

lysosomal enzyme; post translational modification; sulfatase

Indexed keywords

ANIMALIA; CRICETINAE;

EID: 0031568850     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(97)00185-8     Document Type: Article

References (42)

1. Schmidt, B., Selmer, T., Ingendoh, A. & von Figura, K. (1995). A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency. Cell 82, 271-278.
2. McKusick, V. & Neufield, E. (1983). The mucopolysaccharide storage diseases. In The Metabolic Basis of Inherited Disease. (Stanbury, J.B., Wyngaarden, J.B., Frederickson, D.S., Goldstein, J.L. & Brown, M.S., eds), pp. 751-771, McGraw-Hill, NY, USA.
3. Crawley, A.C., et al., & Hopwood, J.J. (1996). Enzyme replacement therapy in a feline model of Maroteaux-Lamy syndrome. J. Clin. Invest. 97, 1864-1873.
4. Sowadski, J.M., Handschumacher, M.D., Krishna Murthy, H.M., Foster, B.A. & Wyckoff, H.W. (1985). Refined structure of alkaline phosphatase from Escherichia coli at 2.8 Å resolution. J. Mol. Biol. 186, 417-433.
5. Holm, L. & Sander, C. (1993). Protein structure comparison by alignment of distance matches. J. Mol. Biol. 233, 123-138.
6. Jones, T.A., Zou, J.-Y., Cowan, S.W. & Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Cryst. A 47, 110-119.
7. Brooks, D.A., et al., & Hopwood, J.J. (1995). Two site-directed mutations abrogate enzyme activity but have different effects on the conformation and cellular content of the N-acetylgalactosamine-4-sulphatase protein. Biochem. J. 307, 457-463.
8. Branden, C.-I. (1980). Relation between structure and function of áâ proteins. Q. Rev. Biophys. 13, 317-338.
9. Roy, A.B. & Mantle, T.J. (1989). The anomalous kinetics of sulphatase A. Biochem. J. 261, 689-697.
10. Anson, D.S., et al., & Hopwood, J.J. (1992). Correction of human mucopolysaccharidosis type-VI fibroblasts with recombinant N-acetylgalactosamine-4-sulphatase. Biochem. J. 284, 789-794.
11. Stewart, D.E., Sarkar, A. & Wampler, J.E. (1990). Occurrence and role of cis peptide bonds in protein structures. J. Mol. Biol. 214, 253-260.
12. Varghese, J.N., Garrett, T.P.J., Colman, P.M., Chen, L. & Hoj, P.B. (1994). Three-dimensional structures of two plant β glucan endohydrolases with distinct substrate specificities. Proc. Natl. Acad. Sci. USA 91, 2785-2789.
13. Perrakis, A., et al., & Vorgias, C.E. (1994). Crystal structure of a bacterial chitinase at 2.3 Å resolution. Structure 2, 1169-1180.
14. Dibbelt, L. & Kuss, E. (1991). Human placental sterylsulfatase. Interaction of the isolated enzyme with substrates, products, transition-state analogues, amino-acid modifiers and anion transport inhibitors. Biol. Chem. Hoppe-Seyler 372, 173-185.
15. Stankiewicz, P.J. & Gresser, M.J. (1988). Inhibition of phosphatase and sulfatase by transition-state analogues. Biochemistry 27, 206-212.
16. Freeman, C. & Hopwood, J.J. (1991). Glucuronate-2-sulphatase activity in cultured human skin fibroblast homogenates. Biochem. J. 279, 399-405.
17. O'Fagain, C., Butler, B.M. & Mantle, T.J. (1983). The effect of pH on the kinetics of arylsulphatases A and B. Biochem. J. 213, 603-607.
18. Essen, L.-O., Perisic, O., Cheung, R., Katan, M. & Williams, R.L. (1996). Crystal structure of a mammalian phosphoinositide-specific phospholipase Cδ. Nature 380, 595-602.
19. Reynolds, C.A., Wade, R.C. & Goodford, P.J. (1989). Identifying targets for bioreductive agents: using GRID to predict selective binding regions of proteins. J. Mol. Graphics 7, 103-108.
20. Hopwood, J.J., Elliott, H., Muller, V.J. & Saccone, G.T.P. (1986). Diagnosis of Maroteaux-Lamy syndrome by the use of radiolabelled oligosaccharides as substrates for the determination of arylsulphatase B activity. Biochem. J. 234, 507-514.
21. Kobayashi, T., Honke, K., Jin, T., Gasa, S., Miyazaki, T. & Makita, A. (1992). Components and proteolytic processing sites of arylsulfatase B from human placenta. Biochim. Biophys. Acta 1159, 243-247.
22. Baranski, T.J., Koelsch, G., Hartsuck, J.A. & Kornfeld, S. (1991). Mapping and molecular modeling of a recognition domain for lysosomal enzyme targeting. J. Biol. Chem. 266, 23365-23372.
23. Baranski, T.J., Faust, P.L. & Kornfeld, S. (1990). Generation of a lysosomal enzyme targeting signal in the secretory protein pepsinogen. Cell 63, 281-291.
24. Jain, S., Drendel, W.B., Chen, Z., Matthews, F.S., Sly, W.S. & Grubb, J.H. (1996). Structure of human beta-glucuronidase reveals candidate lysosomal targeting and active-site motifs. Nat. Struct. Biol. 3, 375-381.
25. Litjens, T., Brooks, D.A., Peters, C., Gibson, G.J. & Hopwood, J.J. (1996). Identification, expression, and biochemical characterization of N-acetylgalactosamine-4-sulfatase mutations and relationship with clinical phenotype in MPS-VI patients. Am. J. Hum. Genet. 58, 1127-1134.
26. Isbrandt, D., Arlt, G., Brooks, DA., Hopwood, J.J., von Figura, K. & Peters, C. (1994). Mucopolysaccharidosis VI (Maroteaux-Lamy syndrome): six unique arylsulfatase B gene alleles causing variable disease phenotypes. Am. J. Hum. Genet. 54, 454-463.
27. Voskoboeva, E., Isbrandt, D., von Figura, K., Krasnopolskaya, X. & Peters, C. (1994). Four novel mutant alleles of the arylsulfatase B gene in two patients with intermediate form of mucopolysaccharidosis VI (Maroteaux-Lamy syndrome). Hum. Genet. 93, 259-264.
28. Jin, W.-D., Jackson, C.E., Desnick, R.J. & Schuchman, E.H. (1992). Mucopolysaccharidosis type VI: identification of three mutations in the arylsulfatase B gene of patients with the severe and mild phenotypes provides molecular evidence for genetic heterogeneity. Am. J. Hum. Genet. 50, 795-800.
29. Wicker, G., et al., & Peters, C. (1991). Mucopolysaccharidosis VI (Maroteaux-Lamy syndrome). An intermediate clinical phenotype caused by substitution of valine for glycine at position 137 of arylsulfatase B. J. Biol. Chem. 266, 21386-21391.
30. Ashby, S.J., Clements, P.R., Guss, J.M., Harvey, I. & Hopwood, J.J. (1995). Crystallization and preliminary characterization of human recombinant N-acetylgalactosamine-4-sulfate sulfatase. Acta Cryst. D 51, 1082-1083.
31. Sakabe, N. (1991). X-ray diffraction data collection system for modern protein crystallography with a Weissenberg camera and an imaging plate using synchrotron radiation. Nucl. Instrum. Meth. Phys. Res. A 303, 448-463.
32. Otwinowski, Z. (1993). Oscillation data reduction program. In Proceedings of the CCP4 Study Weekend: Data Collection and Processing. (Sawyer, L., Isaacs, N. & Bailey, S.S., eds), pp. 56-62, SERC Daresbury Laboratory, Warrington, UK.
33. Collaborative Computational Project No. 4. (1994). The CCP4 suite: programs for protein crystallography. Acta Cryst. D 50, 760-763.
34. Rost, B. (1996). Phd: predicting one-dimensional protein structure by profile based neural networks. Methods Enzymol. 266, 525-539.
35. Brünger, A.T. (1992). X-PLOR, Version 3.1. A System for Crystallography and NMR. Yale University Press, New Haven, CT, USA.
36. Engh, R.A. & Huber, R. (1991). Accurate bond length and angle parameters for X-ray protein structure refinement. Acta Cryst. A 47, 392-400.
37. Kolodny, E.H. & Mumford, R.A. (1976). Human leukocyte acid hydrolases: characterization of eleven lysosomal enzymes and study of reaction conditions for their automated analysis. Clin. Chim. Acta 70, 247-257.
38. Barton, G.J. (1993). ALSCRIPT: a tool to format multiple sequence alignments. Protein Eng. 6, 37-40.
39. Kraulis, P.J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structure. J. Appl. Cryst. 24, 946-950.
40. Merritt, E.A. & Murphy, M.E.P. (1994). RASTER3D Version 2.0: a program for photorealistic molecular graphics. Acta Cryst. D 50, 869-873.
41. Bacon, D.J. & Anderson, W.F. (1988). A fast algorithm for rendering space-filling molecule pictures. J. Mol. Graphics 6, 219-220.
42. Nicholls, A., Bharadwaj, R. & Honig, B. (1993). GRASP: graphical representation and analysis of surface properties. Biophys. J. 64, 166-170.