Solution structure of a single-domain thiosulfate sulfurtransferase from Arabidopsis thaliana

Protein Science

Volumn 15, Issue 12, 2006, Pages 2836-2841

  Cornilescu, Gabriel ^a   Vinarov, Dmitriy A ^a   Tyler, Ejan M ^a   Markley, John L ^a   Cornilescu, Claudia C ^a  

^a UNIVERSITY OF WISCONSIN MADISON   (United States)

Author keywords

At5g66040.1; Center for Eukaryotic Structural Genomics; CESG; NMR; Rhodanese; Single domain sulfurtransferase

Indexed keywords

CYSTEINE; HEAT SHOCK PROTEIN; OXIDOREDUCTASE; PROTEIN TYROSINE PHOSPHATASE; SULFIDE DEHYDROGENASE; SULFURTRANSFERASE; THIOSULFATE SULFURTRANSFERASE;

AMINO ACID SEQUENCE; ARABIDOPSIS; ARTICLE; BINDING AFFINITY; ENZYME SPECIFICITY; ENZYME STRUCTURE; GENE SEQUENCE; GENE STRUCTURE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN DATA BANK; PROTEIN SECONDARY STRUCTURE;

AMINO ACID SEQUENCE; ARABIDOPSIS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID; SOLUTIONS; STRUCTURAL HOMOLOGY, PROTEIN; THIOSULFATE SULFURTRANSFERASE;

ARABIDOPSIS; ARABIDOPSIS THALIANA; EUKARYOTA;

EID: 33751528184     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.062395206     Document Type: Article

References (20)

1. Bauer, M. and Papenbrock, J. 2002. Identification and characterization of single-domain thiosulfate sulfurtransferases from Arabidopsis thaliana. FEBS Lett. 532: 427-431.
2. Bauer, M., Dietrich, C., Nowak, K., Sierralta, W.D., and Papenbrock, J. 2004. Intracellular localization of Arabidopsis sulfurtransferases. Plant Physiol. 135: 916-926.
3. Cornilescu, G., Delaglio, F., and Bax, A. 1999. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 13: 289-302.
4. Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J., and Bax, A. 1995. NMRPIPE - A multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6: 277-293.
5. Garrett, D.S., Powers, R., Gronenborn, A.M., and Clore, G.M. 1991. A common-sense approach to peak picking in two-dimensional, three-dimensional, and four-dimensional spectra using automatic computer-analysis of contour diagrams. J. Magn. Reson. 95: 214-220.
6. Gibrat, J.F., Madej, T., and Bryant, S.H. 1996. Surprising similarities in structure comparison. Curr. Opin. Struct. Biol. 6: 377-385.
7. Hansen, M.R., Mueller, L., and Pardi, A. 1998. Tunable alignment of macromolecules by filamentous phage yields dipolar coupling interactions. Nat. Struct. Biol. 5: 1065-1074.
8. Herrmann, T., Güntert, P., and Wüthrich, K. 2002. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J. Mol. Biol. 319: 209-227.
9. Leon, S., Touraine, B., Ribot, C., Briat, J.F., and Lobreaux, S. 2003. Ironsulphur cluster assembly in plants: Distinct NFU proteins in mitochondria and plastids from Arabidopsis thaliana. Biochem. J. 371: 823-830.
10. Losonczi, J.A. and Prestegard, J.H. 1998. Improved dilute bicelle solutions for high-resolution NMR of biological macromolecules. J. Biomol. NMR 12: 447-451.
11. Nandi, D.L. and Westley, J. 1998. Reduced thioredoxin as a sulfur-acceptor substrate for rhodanese. Int. J. Biochem. Cell Biol. 30: 973-977.
12. Pagani, S., Bonomi, F., and Cerletti, P. 1984. Enzymic-synthesis of the iron-sulfur cluster of spinach ferredoxin. Eur. J. Biochem. 142: 361-366.
13. Ray, W.K., Zeng, G., Potters, M.B., Mansuri, A.M., and Larson, T.J. 2000. Characterization of a 12-kilodalton rhodanese encoded by glpE of Escherichia coli and its interaction with thioredoxin. J. Bacteriol. 182: 2277-2284.
14. Schwieters, C.D. and Clore, G.M. 2001. Internal coordinates for molecular dynamics and minimization in structure determination and refinement. J. Magn. Reson. 152: 288-302.
15. Schwieters, C.D., Kuszewski, J.J., Tjandra, N., and Clore, G.M. 2003. The Xplor-NIH NMR molecular structure determination package. J. Magn. Reson. 160: 65-73.
16. Spallarossa, A., Donahue, J.L., Larson, T.J., Bolognesi, M., and Bordo, D. 2001. Escherichia coli GlpE is a prototype sulfurtransferase for the single-domain rhodanese homology superfamily. Structure 9: 1117-1125.
17. Vennesland, B., Castric, P.A., Conn, E.E., Solomonson, L.P., Volini, M., and Westley, J. 1982. Cyanide metabolism. Fed. Proc. 41: 2639-2648.
18. Vinarov, D.A., Lytle, B.L., Peterson, F.C., Tyler, E.M., Volkman, B.F., and Markley, J.L. 2004. Cell-free protein production and labeling protocol for NMR-based structural proteomics. Nat. Methods 1: 149-153.
19. Westley, J. 1973. Rhodanese. Adv. Enzymol. Relat. Areas Mol. Biol. 39: 327-368.
20. Wüthrich, K. 1986. NMR of proteins and nucleic acids. Wiley Interscience, New York, NY.