Crystal structure of tyrosine hydroxylase at 2.3 Å and its implications for inherited neurodegenerative diseases

Nature Structural Biology

Volumn 4, Issue 7, 1997, Pages 578-585

  Goodwill, Kenneth E ^a   Sabatier, Christelle ^a   Marks, Cara ^a,c   Raag, Reetta ^a   Fitzpatrick, Paul F ^b   Stevens, Raymond C ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b TEXAS A AND M UNIVERSITY   (United States)

^c UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATECHOLAMINE; IRON; LEVODOPA; PHENYLALANINE 4 MONOOXYGENASE; TRYPTOPHAN HYDROXYLASE; TYROSINE 3 MONOOXYGENASE;

ARTICLE; CRYSTAL STRUCTURE; DEGENERATIVE DISEASE; ENZYME ACTIVE SITE; HUMAN; NONHUMAN; PARKINSONISM; PHENYLKETONURIA; POINT MUTATION; PRIORITY JOURNAL;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; NERVE DEGENERATION; PROTEIN CONFORMATION; RATS; SEQUENCE HOMOLOGY, AMINO ACID; TYROSINE 3-MONOOXYGENASE;

EID: 0031010420     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb0797-578     Document Type: Article

References (45)

1. Mallet, J. The TIPS/TINS lecture - Catecholamines - from gene regulation to neuropsychiatric disorders. Trends Neurosci. 19, 191-196 (1996).
2. Kaufman, S. Studies on the mechanism of the enzymatic conversion of phenylalanine to tyrosine. J. Biol. Chem. 234, 2677-2682 (1959).
3. Smyth, C. et al. Further tests for linkage of bipolar affective disorder to the tyrosine hydroxylase gene locus on chromosome 11p15 in a new series of multiplex British affective disorder pedigrees. Amer. J. of Psych. 153, 271-274 (1996).
4. Thibaut, F. et al. Association of DNA polymorphism in the first intron of the tyrosine hydroxylase gene with disturbances of the catecholaminergic system in schizophrenia. Schizophrenia Res. 23, 259-264 (1997).
5. Ludecke, B. et al. Recessively inherited L-DOPA responsive parkinsonism in infancy caused by a point mutation (L205P) in the tyrosine hydroxylase gene. Hum. Mol. Gen. 7, 1023-1028 (1996).
6. Ludecke, B., Dworniczak, B., Bartholome, K. A point mutation in the tyrosine hydroxylase gene associated with Segawa's syndrome. Hum. Genet. 95, 123-125 (1995).
7. Fitzpatrick, P.F. Steady-state kinetic mechanism of rat tyrosine hydroxylase. Biochemistry 30, 3658-3662 (1991).
8. Fitzpatrick, P.F. Kinetic isotope effects on hydroxylation of ring-deuterated phenylalanines by tyrosine hydroyxlase provide evidence against partitioning of an arene oxide intermediate. J. Am. Chem. Soc. 116, 1133-1134 (1994).
9. Hillas, P.J. and Fitzpatrick, P.F. A mechanism for hydroxylation by tyrosine hydroxylase based on partitioning of substituted phenylalanines. Biochemistry 35, 6969-6975 (1996).
10. Hufton, S.E., Jennings, I.G., Cotton, R.G.H. Structure and function of the aromatic amino acid hydroxylases. Biochem. J. 311, 353-366 (1995).
11. Fitzpatrick, P.F. Studies of the rate-limiting step in the tyrosine hydroxylase reaction: alternate substrates, solvent isotope effects, and transition-state analogues. Biochemistry 30, 6386-6391 (1991).
12. Daubner, S.C., Lohse, D.L., Fitzpatrick, P.F. Expression and characterization of the catalytic and regulatory domains of rat tyrosine hydroxylase. Prot. Sci. 2, 1452-1460 (1993).
13. Rost, B., PHD: Predicting one-dimensional protein structure by profile-based neural networks. Meth.Enz. 226, 525-539 (1996).
14. Dickson, P.W., Jennings, I.G., Cotton, R.G.H. Delineation of the catalytic core of phenylalanine hydroxylase and identification of glutamate 286 as a critical residue for pterin function. J. Bio. Chem. 269, 20369-20375 (1994).
15. Vrana, K.E., Walker, S.J., Rucker, P., Liu, X. A carboxyl terminal leucine zipper is required for tyrosine hydroxylase tetramer formation. J. Neurochem. 63, 2014-2020 (1994).
16. Lohse, D.L., Fitzpatrick, P.F. Identification of the intersubunit binding region in rat tyrosine hydroxylase. Biochem. Biophys. Res. Com. 197, 1543-1548 (1993).
17. Lupas, A. Coiled coils: new structures and new functions. Trends Biochem. Sci. 21, 375-382 (1996).
18. Bennett, M.J., Schlunegger, M.P., Eisenberg, D. 3D domain swapping - A mechanism for oligomer assembly. Prot. Sci. 4, 2455-2468 (1995).
19. Quinsey, N.S., Lenaghan, C.M., Dickson, P.W. Identification of Gln(313) and Pro(327) as residues critical for substrate inhibition in tyrosine hydroxylase. J. Neurochem. 66, 908-914 (1996).
20. The FSSP database [Holm, L., Ouzounis. C., Sander, C., Tuparev, G., Vriend, G., Protein Sci. 1, 1691-1698 (1992); Holm, L. and Sander, C., Nucleic Acids Res. 22, 3600-3609 (1994)] is a compilation of representative 3-D protein structures based on an automated analysis of the Protein Data Bank [Bernstein, F.C. et al. , J. Mol. Biol. 233, 123 (1993)].
21. The FSSP database [Holm, L., Ouzounis. C., Sander, C., Tuparev, G., Vriend, G., Protein Sci. 1, 1691-1698 (1992); Holm, L. and Sander, C., Nucleic Acids Res. 22, 3600-3609 (1994)] is a compilation of representative 3-D protein structures based on an automated analysis of the Protein Data Bank [Bernstein, F.C. et al. , J. Mol. Biol. 233, 123 (1993)].
22. The FSSP database [Holm, L., Ouzounis. C., Sander, C., Tuparev, G., Vriend, G., Protein Sci. 1, 1691-1698 (1992); Holm, L. and Sander, C., Nucleic Acids Res. 22, 3600-3609 (1994)] is a compilation of representative 3-D protein structures based on an automated analysis of the Protein Data Bank [Bernstein, F.C. et al. , J. Mol. Biol. 233, 123 (1993)].
23. Iwaki, M. Phillips, R.S., Kaufman, S. Proteolytic modification of the amino-terminal and carboxyl-terminal regions of rat hepatic phenylalanine hydroxylase. 261, 2051-2056 (1986).
24. Ramsey, A.J., Daubner, S.C., Ehrlich, J.I., Fitzpatrick, P.F. Identification of iron ligands in tyrosine hydroxylase by mutagenesis of conserved histidine residues. Prof. Sci. 4, 2082-2086 (1985).
25. Meyerklaucke, W. et al. . Mossbauer, electron-paramagnetic-resonance and X-ray absorption fine-structure studies of the iron environment in recombinant tyrosine hydroxylase. Eur. J. Biochem. 241, 432-439 (1996).
26. Ramsey, A.J., Hillas, P.J., Fitzpatrick, P.F. Characterization of the active site iron in tyrosine hydroxylase - redox states of the iron. J. Bio. Chem. 271, 24395-24400 (1996).
27. Man, S., Eltis, L.D., Timmis, K.M., Muchmore, S.W., Bolin, J.T. Crystal structure of the biphenyl-cleaving extradiol dioxygenase from a PCB-degrading pseudomonad. Science 270, 976-980 (1995).
28. Senda, T. et al. Three-dimensional structures of free form and two substrate complexes of an extradiol ring-cleavage type dioxygenase, the BPHC enzyme from pseudomonas SP strain KKS102. J. Mol. Biol. 255, 735-752 (1996).
29. Quinsey, N.S., Lenaghan, C.M, Dickson, P.W. Identification of Gln(313) and Pro(327) as residues critical for substrate inhibition. J. Neurochem. 66, 908-914 (1996).
30. Knappskogg, P.M., Flatmark, T., Mallet, J. Ludecke, B., Bartholome, K. Recessively inherited L-DOPA-responsive dystonia caused by a point mutation (Q381K) in the tyrosine hydroxylase gene. Hum. Mol. Gen. 4, 1209-1212 (1995).
31. Eisensmith, R.C., Woo, S.L.C., Molecular genetics of PKU: from molecular anthropology to gene therapy. Adv. Genetics 32, 199-271 (1995).
32. Hendrickson, W.A., Horton, J.R., LeMaster, D.M. Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD) - A vehicle for direct determination of 3-dimensional structure. EMBO J. 9, 1665-1672 (1990).
33. Otwinowski, Z., in Data Collection and Processing (eds L. Sawyer, N. Isaacs, S. Bailey) 56562 (Science and Engineering Research Council, Warrington, UK; 1993).
34. CCP4: A Suite of Programs for Protein Crystallography (SERC Daresbury Laboratory, Warrington WA44AD, UK, 1979).
35. McRee, D.E. A visual protein crystallographic software system for X11/Xview J. Mol. Graphics 10, 44 (1992).
36. Otwinowski, Z., in Proceedings of the CCP4 Study Weekend: Isomorphous Replacement and Anomalous Scattering (eds W. Wolf, RR. Evans, A.G.W. Leslie) 80886 (SERC Daresbury Laboratory, Warrington, UK; 1991).
37. Cowtan, K.D. Improvement of macromolecular electron-density maps by the simultaneous application of real and reciprocal space constraints. Acta Crystallogr. D49, 148-157 (1993).
38. Jones, T.A., Zou, J.-Y, Cowan, S.W., KKjelgaard, M. Improved methods for the building of protein models in electron density maps and the location of errors in these. Acta Crystallogr. A47, 110-119 (1991).
39. Brünger, A.T., X-PLOR v3.8, Yale Univ. Press, New Haven, CT (1996).
40. Colovos, C., Yeates, T.O. Verification of protein structures - Patterns of nonbonded atomic interactions. Prot. Sci. 2, 1511-1519 (1993).
41. Laskowski, R.A., MacArthus, M.W., Moss, D.S., Thornton, J.M. PROCHECK - A program to check the stereochemical quality of protein structures. J. Applied Crystallogr. 26, 283-291 (1993).
42. Vriend, G., What If: A molecular modeling and drug design program. J. Mol. Graphics 8, 52-56 (1990).
43. Kabsch, W., Sander, C., Dictionary of protein secondary structure: pattern recognition of hydrogen bonded and geometrical features. Biopolymers 22, 2577-2637 (1983).
44. Kraulis, P.J. MOLSCRIPT - A program to produce both detailed and schematic plots of protein structures. J. Appl Crystallogr 24, 946-950 (1991).
45. Merritt, E.A., Murphy, M.E.P. Raster3D Version 2.0. A program for photorealistic molecular graphics. Acta Crystallogr. D50, 869-873 (1994).