Structure of the molybdopterin-bound Cnx1G domain links molybdenum and copper metabolism

Nature

Volumn 430, Issue 7001, 2004, Pages 803-806

  Kuper, Jochen ^a,c   Llamas, Angel ^a   Hecht, Hans Jürgen ^b   Mendel, Ralf R ^a   Schwarz, Günter ^a  

^a TECHNICAL UNIVERSITY OF BRAUNSCHWEIG   (Germany)

^b HELMHOLTZ CENTRE FOR INFECTION RESEARCH   (Germany)

^c DESY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

BIOSYNTHESIS; CATALYSIS; COPPER; ENZYMES; METABOLISM; MOLYBDENUM;

MOLYBDENUM COFACTORS; NITROGENASE;

NATURAL SCIENCES;

COPPER; MOLYBDENUM; MOLYBDOPTERIN; NITROGENASE; PROTEIN; PROTEIN CNX1G; PTERIN DERIVATIVE; PYRANOPTERIN; UNCLASSIFIED DRUG; VEGETABLE PROTEIN; ADENOSINE PHOSPHATE; ARABIDOPSIS PROTEIN; CALNEXIN; CNX1 PROTEIN, ARABIDOPSIS; MAGNESIUM; METALLOPROTEIN; MOLYBDENUM COFACTOR; PTERIDINE DERIVATIVE; SULFUR;

MOLYBDENUM;

ADENYLATION; AMINO TERMINAL SEQUENCE; ARTICLE; BIOSYNTHESIS; COMPLEX FORMATION; CONTROLLED STUDY; COPPER METABOLISM; CRYSTAL STRUCTURE; METAL BINDING; MOLECULAR BIOLOGY; PLANT; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN PHOSPHORYLATION; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; COENZYME; CRYSTALLIZATION; METABOLISM; PROTEIN TERTIARY STRUCTURE; X RAY CRYSTALLOGRAPHY;

INSERTION SEQUENCES; PIERIDAE;

ADENOSINE MONOPHOSPHATE; ARABIDOPSIS PROTEINS; BINDING SITES; CALNEXIN; COENZYMES; COPPER; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; MAGNESIUM; METALLOPROTEINS; MODELS, MOLECULAR; MOLYBDENUM; PLANT PROTEINS; PLANTS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; PTERIDINES; SULFUR;

EID: 4043114792     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature02681     Document Type: Article

References (30)

1. Hille, R. The mononuclear molybdenum enzymes. Chem. Rev. 96, 2757-2816 (1996).
2. Roman, M. J. et al. Crystal structure of the xanthine oxidase-related aldehyde oxido- reductase from D. gigas. Science 270, 1170-1176 (1995).
3. Chan, M. K., Mukund, S., Kletzin, A., Adams, M. W. W. & Rees, D. C. Structure of a hyperthermophilic tungstopterin, aldehyde ferredoxin oxidoreductase. Science 267, 1463-1469 (1995).
4. Mendel, R. R. & Schwarz, G. Biosynthesis and molecular biology of the molybdenum cofactor (Moco). Met. Ions Biol. Syst. 39, 317-368 (2002).
5. Stiefel, E. I. Molybdenum bolsters the bioinorganic brigade. Science 272, 1599-1600 (1996).
6. Enemark, J. H. & Cosper, M. M. Molybdenum enzymes and sulfur metabolism. Met. Ions Biol. Syst. 39, 621-654 (2002).
7. Mendel, R. R. & Schwarz, G. Molybdoenzymes and molybdenum cofactor in plants. Crit. Rev. Plant. Sci. 18, 33-69 (1999).
8. Johnson, J. L. et al. Inborn errors of molybdenum metabolism: combined deficiencies of sulfite oxidase and xanthine dehydrogenase in a patient lacking the molybdenum cofactor. Proc. Natl Acad. Sci. USA 77, 3715-3719 (1980).
9. Shih, V. E. et al. Sulfite oxidase deficiency. Biochemical and clinical investigations of a hereditary metabolic disorder in sulfur metabolism. N. Engl. J. Med. 297, 1022-1028 (1977).
10. Kuper, J., Winking, J., Hecht, H. J., Mendel, R. R. & Schwarz, G. The active site of the molybdenum cofactor biosynthetic protein domain Cnx1G. Arch. Biochem. Biophys. 411, 36-46 (2003).
11. Schwarz, G. et al. The molybdenum cofactor biosynthetic protein Cnx1 complements molybdate-repairable mutants, transfers molybdenum to the metal binding pterin, and is associated with the cytoskeleton. Plant Cell 12, 2455-2472 (2000).
12. Kuper, J. et al. In vivo detection of molybdate-binding proteins using a competition assay with ModE in Escherichia coli. FEMS Microbiol. Lett. 218, 187-193 (2003).
13. Kisker, C. et al. Molecular basis of sulfite oxidase deficiency from the structure of sulfite oxidase. Cell 91, 973-983 (1997).
14. Kuper, J., Palmer, T., Mendel, R. R. & Schwarz, G. Mutations in the molybdenum cofactor biosynthetic protein Cnx1G from Arabidopsis thaliana define functions for molybdopterin bind, Mo-insertion and molybdenum cofactor stabilization. Proc. Natl Acad. Sci. USA 97, 6475-6480 (2000).
15. Lake, M. W., Wuebbens, M. M., Rajagopalan, K. V. & Schindelin, H. Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex. Nature 414, 325-329 (2001).
16. Schindelin, H., Kisker, C., Hilton, J., Rajagopalan, K. V. & Rees, D. C. Crystal structure of DMSO reductase: redox-linked changes in molybdopterin coordination. Science 272, 1615-1621 (1996).
17. Schrader, N. et al. The crystal structure of plant sulfite oxidase provides insights into sulfite oxidation in plants and animals. Structure 11, 1251-1263 (2003).
18. Santamaria-Araujo, J. A. et al. The tetrahydropyranopterin structure of the sulfur-free and metal-free molybdenum cofactor precursor. J. Biol. Chem. 279, 15994-15999 (2004).
19. Bertero, M. G. et al. Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A. Nature Struct. Biol. 10, 681-687 (2003).
20. Nason, A. et al. In vitro formation of assimilatory reduced nicotinamide adenine dinucleotide phosphate: nitrate reductase from a Neurospora mutant and a component of molybdenum-enzymes. Proc. Natl Acad. Sci. USA 68, 3242-3246 (1971).
21. Xiang, S., Nichols, J., Rajagopalan, K. V. & Schindelin, H. The crystal structure of Escherichia coli MoeA and its relationship to the multifunctional protein Gephyrin. Structure 9, 299-310 (2001).
22. Schrag, J. D. et al. The crystal structure of Escherichia coli MoeA, a protein from the molybdopterin synthesis pathway. J. Mol. Biol. 310, 419-431 (2001).
23. Moorhead, G. B. et al. Purification of a plant nucleotide pyrophosphatase as a protein that interferes with nitrate reductase and glutamine synthetase assays. Eur. J. Biochem. 270, 1356-1362 (2003).
24. Mercer, J. F. The molecular basis of copper-transport diseases. Trends Mol. Med. 7, 64-69 (2001).
25. Mason, J. Thiomolybdates: mediators of molybdenum toxicity and enzyme inhibitors. Toxicology 42, 99-109 (1986).
26. Navaza, J. AMORE-an automated package for molecular replacement. Acta Crystallogr. A 50, 157-163 (1994).
27. Jones, T. A., Zou, J. Y., Cowan, S. W. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119 (1991).
28. Murshudov, G., Vagin, A. & Dodson, E. Refinement of macromolecular structures by the maximum likelihood method. Acta Crystallogr. D 53, 240-255 (1997).
29. Guse, A. et al. Biochemical and structural analysis of the molybdenum cofactor biosynthesis protein MobA. J. Biol. Chem. 278, 25302-25307 (2003).
30. Nicholls, A., Sharp, K. A. & Honig, B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins Struct. Funct. Genet. 11, 281-296 (1991).