Structural insights into the neuroprotective-acting carbonyl reductase Sniffer of Drosophila melanogaster

Journal of Molecular Biology

Volumn 342, Issue 5, 2004, Pages 1613-1624

  Sgraja, Tanja ^a   Ulschmid, Julia ^b   Becker, Katja ^b   Schneuwly, Stephan ^c   Klebe, Gerhard ^a   Reuter, Klaus ^a   Heine, Andreas ^a  

^a PHILIPPS UNIVERSITY MARBURG   (Germany)

^b JUSTUS LIEBIG UNIVERSITY   (Germany)

^c UNIVERSITY OF REGENSBURG   (Germany)

Author keywords

carbonyl reductase; MAD; Sniffer; X ray crystal structure

Indexed keywords

CARBONYL REDUCTASE; DIMER; DINUCLEOTIDE; ENZYME; LIGAND; NEUROPROTECTIVE AGENT; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; OXIDOREDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; SNIFFER PROTEIN; UNCLASSIFIED DRUG;

AGE; ARTICLE; BINDING AFFINITY; BINDING SITE; CONTROLLED STUDY; CRYSTAL STRUCTURE; DEGENERATIVE DISEASE; DISPERSION; DROSOPHILA MELANOGASTER; IN VIVO STUDY; MOLECULAR MODEL; NEUROPROTECTION; NONHUMAN; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN FOLDING; PROTEIN STRUCTURE;

DROSOPHILA MELANOGASTER; MELANOGASTER; SUIDAE;

EID: 4444228337     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.08.020     Document Type: Article

References (49)

1. A.M. Gorman, A. McGowan, C. O'Neill, and T. Cotter Oxidative stress and apoptosis in neurodegeneration J. Neurol. Sci. 139 Suppl 1996 45 52
2. J.B. Schulz, J. Lindenau, J. Seyfried, and J. Dichgans Glutathione, oxidative stress and neurodegeneration Eur. J. Biochem. 267 2000 4904 4911
3. Y. Christen Oxidative stress and Alzheimer disease Am. J. Clin. Nutr. 71 2000 621S 629S
4. M.A. Smith, G. Perry, P.L. Richey, L.M. Sayre, V.E. Anderson, M.F. Beal, and N. Kowall Oxidative damage in Alzheimer's Nature 382 1996 120 121
5. R. Dringen Metabolism and functions of glutathione in brain Prog. Neurobiol. 62 2000 649 671
6. J.A. Botella, J.K. Ulschmid, C. Gruenewald, C. Moehle, D. Kretzschmar, K. Becker, and S. Schneuwly The Drosophila carbonyl reductase Sniffer prevents oxidative stress-induced neurodegeneration Curr. Biol. 14 2004 782 786
7. H. Jornvall, B. Persson, M. Krook, S. Atrian, R. Gonzalez-Duarte, J. Jeffery, and D. Ghosh Short-chain dehydrogenases/reductases (SDR) Biochemistry 34 1995 6003 6013
8. T. Terada, Y. Sugihara, K. Nakamura, R. Sato, N. Inazu, and M. Maeda Cloning and bacterial expression of monomeric short-chain dehydrogenase/ reductase (carbonyl reductase) from CHO-K1 cells Eur. J. Biochem. 267 2000 6849 6857
9. D. Ghosh, M. Sawicki, V. Pletnev, M. Erman, S. Ohno, S. Nakajin, and W.L. Duax Porcine carbonyl reductase. structural basis for a functional monomer in short-chain dehydrogenases/reductases J. Biol. Chem. 276 2001 18457 18463
10. M. Tanaka, S. Ohno, S. Adachi, S. Nakajin, M. Shinoda, and Y. Nagahama Pig testicular 20beta-hydroxysteroid dehydrogenase exhibits carbonyl reductase-like structure and activity. cDNA cloning of pig testicular 20beta-hydroxysteroid dehydrogenase J. Biol. Chem. 267 1992 13451 13455
11. G.M. Morris, D.S. Goodsell, R.S. Halliday, R. Huey, W.E. Hart, R.K. Belew, and A.J. Olson Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function J. Comput. Chem. 19 1998 1632 1662
12. L. Giot, J.S. Bader, C. Brouwer, A. Chaudhuri, B. Kuang, and Y. Li A protein interaction map of Drosophila melanogaster Science 302 2003 1727 1736
13. L. Holm, and C. Sander Protein structure comparison by alignment of distance matrices J. Mol. Biol. 233 1993 123 138
14. D. Ghosh, V.Z. Pletnev, D.W. Zhu, Z. Wawrzak, W.L. Duax, and W. Pangborn Structure of human estrogenic 17beta-hydroxysteroid dehydrogenase at 2.20 Å resolution Structure 3 1995 503 513
15. J. Benach, S. Atrian, R. Gonzalez-Duarte, and R. Ladenstein The refined crystal structure of Drosophila lebanonensis alcohol dehydrogenase at 1.9 Å resolution J. Mol. Biol. 282 1998 383 399
16. J.B. Rafferty, J.W. Simon, C. Baldock, P.J. Artymiuk, P.J. Baker, and A.R. Stuitje Common themes in redox chemistry emerge from the X-ray structure of oilseed rape (Brassica napus) enoyl acyl carrier protein reductase Structure 3 1995 927 938
17. C. Grimm, E. Maser, E. Mobus, G. Klebe, K. Reuter, and R. Ficner The crystal structure of 3alpha-hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni shows a novel oligomerization pattern within the short-chain dehydrogenase/reductase family J. Biol. Chem. 275 2000 41333 41339
18. S. Jones, and J.M. Thornton Principles of protein-protein interactions Proc. Natl Acad. Sci. USA 93 1996 13 20
19. M.L. Connolly Solvent-accessible surfaces of proteins and nucleic acids Science 221 1983 709 713
20. A.M. Lesk NAD-binding domains of dehydrogenases Curr. Opin. Struct. Biol. 5 1995 775 783
21. N. Tanaka, T. Nonaka, T. Tanabe, T. Yoshimoto, D. Tsuru, and Y. Mitsui Crystal structures of the binary and ternary complexes of 7alpha-hydroxysteroid dehydrogenase from Escherichia coli Biochemistry 35 1996 7715 7730
22. D. Ghosh, C.M. Weeks, P. Grochulski, W.L. Duax, M. Erman, R.L. Rimsay, and J.C. Orr Three-dimensional structure of holo 3alpha,20beta-hydroxysteroid dehydrogenase: a member of a short-chain dehydrogenase family Proc. Natl Acad. Sci. USA 88 1991 10064 10068
23. M. Hulsmeyer, H.J. Hecht, K. Niefind, B. Hofer, L.D. Eltis, K.N. Timmis, and D. Schomburg Crystal structure of cis-biphenyl-2,3-dihydrodiol-2,3- dehydrogenase from a PCB degrader at 2.0 Å resolution Protein Sci. 7 1998 1286 1293
24. U.C. Oppermann, C. Filling, K.D. Berndt, B. Persson, J. Benach, R. Ladenstein, and H. Jornvall Active site directed mutagenesis of 3beta/17beta-hydroxysteroid dehydrogenase establishes differential effects on short-chain dehydrogenase/reductase reactions Biochemistry 36 1997 34 40
25. N. Tanaka, T. Nonaka, M. Nakanishi, Y. Deyashiki, A. Hara, and Y. Mitsui Crystal structure of the ternary complex of mouse lung carbonyl reductase at 1.8 Å resolution: the structural origin of coenzyme specificity in the short-chain dehydrogenase/reductase family Structure 4 1996 33 45
26. + identifies two principal targets for the design of inhibitors Structure 4 1996 905 915
27. Z. Chen, J.C. Jiang, Z.G. Lin, W.R. Lee, M.E. Baker, and S.H. Chang Site-specific mutagenesis of Drosophila alcohol dehydrogenase: evidence for involvement of tyrosine 152 and lysine 156 in catalysis Biochemistry 32 1993 3342 3346
28. W.S. Somers, M.L. Stahl, and F.X. Sullivan GDP-fucose synthetase from Escherichia coli: structure of a unique member of the short-chain dehydrogenase/reductase family that catalyzes two distinct reactions at the same active site Structure 6 1998 1601 1612
29. D. Bashford Scientific computing in object-oriented parallel environments Y. Ishikawa R.R. Oldehoeft J.V.W. Reynders T. Marydell Lecture Notes in Computer Science vol. 1343 1997 Springer Berlin 233 240
30. B. Persson, M. Krook, and H. Jornvall Characteristics of short-chain alcohol dehydrogenases and related enzymes Eur. J. Biochem. 200 1991 537 543
31. M.A. Sciotti, S. Nakajin, B. Wermuth, and M.E. Baker Mutation of threonine 241 to proline eliminates autocatalytic modification of human carbonyl reductase Biochem. J. 350 2000 89 92
32. B. Wermuth, K.M. Bohren, G. Heinemann, J.P. von Wartburg, and K.H. Gabbay Human carbonyl reductase. Nucleotide sequence analysis of a cDNA and amino acid sequence of the encoded protein J. Biol. Chem. 263 1988 16185 16188
33. K. Watanabe, C. Sugawara, A. Ono, Y. Fukuzumi, S. Itakura, and M. Yamazaki Mapping of a novel human carbonyl reductase, CBR3, and ribosomal pseudogenes to human chromosome 21q22.2 Genomics 52 1998 95 100
34. G.D. Van Duyne, R.F. Standaert, P.A. Karplus, S.L. Schreiber, and J. Clardy Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin J. Mol. Biol. 229 1993 105 124
35. J. Navaza AMoRe: an automated package for molecular replacement Acta Crystallog. sect. A 50 1994 157 163
36. W.L. DeLano, and A.T. Brunger The direct rotation function: rotational patterson correlation search applied to molecular replacement Acta Crystallog. sect. D 51 1995 740 748
37. C.R. Kissinger, D.K. Gehlhaar, and D.B. Fogel Rapid automated molecular replacement by evolutionary search Acta Crystallog. sect. D 55 1999 484 491
38. A. Vagin, and A. Teplyakov MOLREP: an automated program for molecular replacement J. Appl. Crystallog. 30 1997 1022 1025
39. Z. Otwinowski, and W. Minor Processing of X-ray data diffraction data collected in oscillation mode R.W. Carter R.M. Sweet Methods in Enzymology vol. 276 1996 Academic Press New York 307 326
40. T.R. Schneider, and G.M. Sheldrick Substructure solution with SHELXD Acta Crystallog. sect. D 58 2002 1772 1779
41. G.M. Sheldrick Macromolecular phasing with SHELXE Z. Kristallographie 217 2002 1 7
42. K.D. Cowtan, and K.Y. Zhang Density modification for macromolecular phase improvement Prog. Biophys. Mol. Biol. 72 1999 245 270
43. V.S. Lamzin, and K.S. Wilson Automated refinement of protein models Acta Crystallog. sect. D 49 1993 129 149
44. T.A. Jones, J.Y. Zou, S.W. Cowan, and M. Kjeldgaard Improved methods for building protein models in electron density maps and the location of errors in these models Acta Crystallog. sect. A 47 1991 110 119
45. A.T. Brunger, P.D. Adams, G.M. Clore, W.L. DeLano, P. Gros, and R.W. Grosse-Kunstleve Crystallography and NMR system: a new software suite for macromolecular structure determination Acta Crystallog. sect. D 54 1998 905 921
46. G.M. Sheldrick, and T.R. Schneider SHELXL R.W. Carter R.M. Sweet Methods in Enzymology vol. 277b 1997 Academic Press New York 319 343
47. R.A. Laskowski, M.W. MacArthur, D.S. Moss, and J.M. Thornton PROCHECK: a program to check the stereochemical quality of protein structures J. Appl. Crystallog. 26 1993 283 291
48. E.G. Hutchinson, and J.M. Thornton PROMOTIF - a program to identify and analyze structural motifs in proteins Protein Sci. 5 1996 212 220
49. A.D. McLachlan Rapid comparison of protein structures Acta Crystallog. sect. D 38 1982 871 873