Molecular basis of glutathione synthetase deficiency and a rare gene permutation event

EMBO Journal

Volumn 18, Issue 12, 1999, Pages 3204-3213

  Polekhina, Galina ^a   Board, Philip G ^b   Gali, Rayappa R ^b   Rossjohn, Jamie ^a   Parker, Michael W ^a  

^a ST VINCENT'S INSTITUTE OF MEDICAL RESEARCH   (Australia)

^b AUSTRALIAN NATIONAL UNIVERSITY   (Australia)

Author keywords

ATP grasp superfamily; Genetic disease; Glutathione; Glutathione synthetase; X ray crystallography

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; GLUTATHIONE; GLUTATHIONE SYNTHASE; MAGNESIUM ION; SULFATE;

ARTICLE; CRYSTAL STRUCTURE; ENZYME DEFICIENCY; ENZYME MECHANISM; EVOLUTION; GENE MUTATION; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE; SEQUENCE HOMOLOGY;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; BINDING SITES; CONSERVED SEQUENCE; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; EVOLUTION, MOLECULAR; GENES; GLUTATHIONE; GLUTATHIONE SYNTHASE; HUMANS; MAGNESIUM; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PHOSPHATES; PROTEIN STRUCTURE, SECONDARY; SULFATES;

EID: 0033564203     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/18.12.3204     Document Type: Article

References (32)

1. Anderson, M.E. (1998) Glutathione: an overview of biosynthesis and modulation. Chem. Biol. Interact., 111-112, 1-14.
2. Artymiuk, P.J., Poirrette, A.R., Rice, D.W. and Willett, P. (1996) Biotin carboxylase comes into the fold. Nature Struct. Biol., 3, 128-132.
3. Barton, G.J. (1993) ALSCRIPT - a tool to format multiple sequence alignments. Protein Eng., 6, 37-40.
4. Collaborative Computational Project Number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr., D50, 760-763.
5. Dahl, N., Pigg, M., Ristoff, E., Gali, R., Carlsson, B., Mannervik, B., Larsson, A. and Board, P. (1997) Missense mutations in the human glutathione synthetase gene result in severe metabolic acidosis, 5-oxoprolinuria, hemolytic anemia and neurological dysfunction. Human Mol. Genet., 6, 1147-1152.
6. Esser, L., Wang, C.-R., Hosaka, M., Smagula, C.S., Südhof, T.C and Deisenhofer, J. (1998) Synapsin I is structurally similar to ATP-utilizing enzymes. EMBO J., 17, 977-984.
7. Fan, C., Moews, P.C., Walsh, C.T. and Knox, J.R. (1994) Vancomycin resistance: Structure of D-alanine:D-alanine ligase at 2.3 Å resolution. Science, 266, 439-443.
8. Fan, C., Moews, P.C., Shi, Y., Walsh, C.T. and Knox, J.R. (1995) A common fold for peptide synthetases cleaving ATP to ADP: glutathione synthetase and D-alanine:D-alanine ligase of Escherichia coli. Proc. Natl Acad. Sci. USA, 92, 1172-1176.
9. Gali, R.R. and Board, P.G. (1995) Sequencing and expression of a cDNA for human glutathione synthetase. Biochem. J., 310, 353-358.
10. Gali, R.R. and Board, P.G. (1997) Identification of an essential cysteine residue in human glutathione synthase. Biochem. J., 321, 207-210.
11. Galperin, M.Y. and Koonin, E.V. (1997) A diverse superfamily of enzymes with ATP-dependent carboxylate-amine/thiol ligase activity. Protein Sci., 6, 2639-2643.
12. Gruer, M.J., Artymiuk, P.J. and Guest, J.R. (1997) The aconitase family: three structural variations on a common theme. Trends Biochem. Sci., 22, 3-6.
13. Gushima, H., Yasuda, S., Soeda, E., Yokota, M. and Kimura, A. (1984) Complete nucleotide sequence of the E.coli glutathione synthetase gsh-II. Nucleic Acids Res., 12, 9299-9307.
14. Hara, T., Kato, H., Katsube Y. and Oda, J. (1996) A pseudo-Michaelis quaternary complex in the reverse reaction of a ligase: structure of Escherichia coli B glutathione synthetase complexed with ADP, glutathione and sulfate at 2.0 Å resolution. Biochemistry, 35, 11967-11974.
15. Jones, T.A., Zou, J.-Y., Cowan, S.W. and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of error in these models. Acta Crystallogr., A42, 110-119.
16. Kraulis, P.J. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of proteins. J. Appl. Crystallogr., 24, 946-950.
17. Laskowski, R.A., MacArthur, M.W., Moss, D.S. and Thornton, J.M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr., 26, 283-291.
18. Leslie, A.G.W. (1992) Recent changes to the MOSFLM package for processing film and image plate data. In Wolf, W.M. and Wilson, K.S. (eds), Joint CCP4 and ESF-EACMB Newsletter on Protein Crystallography No. 26. SERC Laboratory, Daresbury, Warrington, UK.
19. Lindqvist, Y. and Schneider, G. (1997) Circular permutations of natural protein sequences: structural evidence. Curr. Opin. Struct. Biol., 7, 422-427.
20. Lüthy, R., Bowie, J.U. and Eisenberg, D. (1992) Assessment of protein models with 3-dimensional profiles. Nature, 356, 83-85.
21. Meister, A. and Larsson, A. (1995) Glutathione synthetase deficiency and other disorders of the γ-glutamyl cycle. In Scriver, C.R., Beaudet, A.L., Sly, W.S. and Valle D. (eds), The Metabolic Basis of Inherited Diseases. 7th edn. Wiley, New York, NY, pp. 1461-1477.
22. Murzin, A.G. (1996) Structural classification of proteins: new superfamilies. Curr. Opin. Struct. Biol., 6, 386-394.
23. Murshudov, G.N., Vagin, A.A. and Dodson, E.J. (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr., D53, 240-255.
24. Otwinowski, Z. and Minor, W. (1997) Processing X-ray diffraction data collected in oscillation mode. Methods Enzymol., 276, 307-326.
25. Ristoff, E. and Larsson, A. (1998) Patients with genetics defects in the γ-glutamyl cycle. Chem. Biol. Interact., 111-112, 113-121.
26. Shi, Z.Z., Habib, G.M., Rhead, W.J., Gahl, W.A., He, X., Sazer, S. and Lieberman, M.W. (1996) Mutations in the glutathione synthetase gene cause 5-oxoprolinuria. Nature Genet., 14, 362-365.
27. Thoden, J.B., Holden, H.M., Wesenberg, G., Raushel, F.M. and Rayment, I. (1997) Structure of carbamoyl phosphate synthetase: A journey of 96 Å from substrate to product. Biochemistry, 36, 6305-6316.
28. Waldrop, G.L., Rayment, I. and Holden, H.M. (1994) Three-dimensional structure of the biotin carboxylase subunit of acetyl-CoA carboxylase. Biochemistry, 33, 10249-10256.
29. Webb, G.C., Vaska, V.L., Gali, R.R., Ford, J.H. and Board, P.G. (1995) The gene encoding human glutathione synthetase (GSS) maps to the long arm of chromosome 20 at band 11.2. Genomics, 30, 617-619.
30. Whitbread, L., Gali, R.R. and Board, P.G. (1998) The structure of the human glutathione synthetase gene. Chem. Biol. Interact., 111-112, 35-40.
31. Wolodko, W.T., Fraser, M.E., James, M.N.G. and Bridger, W.A. (1994) The crystal structure of succinyl-CoA synthetase from Escherichia coli at 2.5 Å resolution. J. Biol. Chem., 269, 10883-10890.
32. Yamaguchi, H., Kato, H., Hata, Y., Nishioka, T., Kimura, A., Oda, J. and Katsube, Y. (1993) Three-dimensional structure of the glutathione synthetase from Escherichia coli B at 2.0 Å resolution. J. Mol. Biol., 229, 1083-1100.