Crystal structure of IscS, a cysteine desulfurase from Escherichia coli

Journal of Molecular Biology

Volumn 330, Issue 5, 2003, Pages 1049-1059

  Cupp Vickery, Jill R ^a   Urbina, Hugo ^a   Vickery, Larry E ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Crystal structure; Cysteine desulfurase; IscS; NifS; Pyridoxal phosphate

Indexed keywords

BACTERIAL ENZYME; CYSTATHIONINE GAMMA LYASE; CYSTEINE;

ARTICLE; CATALYSIS; CONTROLLED STUDY; DESULFURIZATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ASSAY; ENZYME CONFORMATION; ENZYME STRUCTURE; ENZYME SUBUNIT; ESCHERICHIA COLI; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN SECONDARY STRUCTURE; STRUCTURAL HOMOLOGY; STRUCTURE ANALYSIS; THERMOTOGA MARITIMA;

ESCHERICHIA COLI; THERMOTOGA; THERMOTOGA MARITIMA;

EID: 0038351831     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00690-9     Document Type: Article

References (44)

1. Beinert H., Holm R.H., Munck E. Iron-sulfur clusters: nature's modular, multipurpose structures. Science. 277:1997;653-659.
2. Johnson M.K. Iron-sulfur proteins: new roles for old clusters. Curr. Opin. Chem. Biol. 2:1998;173-181.
3. Beinert H. Iron-sulfur proteins: ancient structures, still full of surprises. J. Biol. Inorg. Chem. 5:2000;2-15.
4. Zheng L., White R.H., Cash V.L., Jack R.F., Dean D.R. Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis. Proc. Natl Acad. Sci. USA. 90:1993;2754-2758.
5. Zheng L., White R.H., Cash V.L., Dean D.R. Mechanism for the desulfurization of L-cysteine catalyzed by the nifS gene product. Biochemistry. 33:1994;4714-4720.
6. Zheng L., Dean D.R. Catalytic formation of a nitrogenase iron-sulfur cluster. J. Biol. Chem. 26:1994;18723-18726.
7. Zheng L., Cash V.L., Flint D.H., Dean D.R. Assembly of iron-sulfur clusters. Identification of and iscSUA-hscBA-fdx gene cluster from Azotobacter vinelandii. J. Biol. Chem. 273:1998;13264-13272.
8. Strain J., Lorenz C.R., Bode J., Garland S., Smolen G.A., Ta D.T., et al. Suppressors of superoxide dismutase (SOD1 deficiency in Saccharomyces cerevisiae. Identification of proteins predicted to mediate iron-sulfur cluster assembly. J. Biol. Chem. 273:1998;31138-31144.
9. Li J., Kogan M., Knight S.A.B., Pain D., Dancis A. Yeast mitochondrial protein, Nfs1p, coordinately regulates iron-sulfur proteins, cellular iron uptake, and iron distribution. J. Biol. Chem. 274:1998;33025-33034.
10. Schwartz C.J., Djaman O., Imlay J.A., Kiley P.J. The cysteine desulfurase, IscS, has a major role in in vivo Fe-S cluster formation in Escherichia coli. Proc. Natl Acad. Sci. USA. 97:2000;9009-9014.
11. Jaschkowitz K., Seidler A. Role of a NifS-like protein from the cyanobacterium Synechocystis PCC 6803 in the maturation of FeS proteins. Biochemistry. 39:2000;3416-3423.
12. Mihara H., Esaki N. Bacterial cysteine desulfurases: their function and mechanisms. Appl. Microbiol. Technol. 60:2002;12-23.
13. Flint D.H. Escherichia coli contains a protein that is homologous in function and N-terminal sequence to the protein encoded by the nifS gene of Azotobacter vinelandii and that can participate in the synthesis of dihydroxy-acid dehydratase. J. Biol. Chem. 271:1996;16068-16074.
14. Khoroshilova N., Beinert H., Kiley P.J. Association of a polynuclear iron-sulfur center with a mutant FNR protein enhances DNA binding. Proc. Natl Acad. Sci. USA. 92:1995;2499-2503.
15. Chen S., Zheng L., Dean D.R., Zalkin H. Role of NifS in maturation of glutamine phosphoribosylpyrophosphate amidotransferase. J. Bacteriol. 179:1997;7587-7590.
16. Hidalgo E., Demple B. Activation of SoxR-dependent transcription in vitro by noncatalytic or NifS-mediated assembly of [2Fe-2S] clusters into apo-SoxR. J. Biol. Chem. 271:1996;7269-7272.
17. Bui B.T.B., Escalettes F., Chottard G., Florentin D., Marquet A. Enzyme-mediated sulfide production for the reconstitution of [2Fe-2S] clusters into apo-biotin synthase of Escherichia coli. Eur. J. Biochem. 267:2000;2688-2694.
18. Yuvaniyama P., Agar J.N., Cash V.L., Johnson M.K., Dean D.R. NifS-directed assembly of a transient [2Fe-2S] cluster within the NifU protein. Proc. Natl Acad. Sci. USA. 97:2000;599-604.
19. 2] cluster in IscU. J. Am. Chem. Soc. 122:2000;2136-2137.
20. Urbina H.D., Silberg J.J., Hoff K.G., Vickery L.E. Transfer of sulfur from IscS to IscU during Fe-S cluster assembly. J. Biol. Chem. 276:2001;44521-44526.
21. Kambampati R., Lauhon C.T. IscS is a sulfurtransferase for the in vivo biosynthesis of 4-thiouridine in Escherichia coli tRNA. Biochemistry. 38:1999;16561-16568.
22. Lauhon C.T., Kambapati R. The iscS gene in Escherichia coli is required for the biosynthesis of 4-thioruridine, thiamine, and NAD. J. Biol. Chem. 275:2000;20096-20103.
23. Lauhon C.T. Requirement for IscS in biosynthesis of all thionucleosides in Escherichia coli. J. Bacteriol. 184:2002;6820-6829.
24. Nilsson K., Lundgren H.K., Hagervall T.G., Bjork G.R. The cysteine desulfurase IscS is required for synthesis of all five thiolated nucleosides present in tRNA from Salmonella enterica serovar typhimurium. J. Bacteriol. 184:2002;6830-6835.
25. Kiyasu T., Asakura A., Nagahashi Y., Hoshino T. Contribution of cysteine desulfurase (NifS protein) to the biotin synthase reaction of Escherichia coli. J. Bacteriol. 182:2000;2879-2885.
26. Kaiser J.T., Clausen T., Bourenkow G.P., Bartunik H.-D., Steinbacher S., Huber R. Crystal structure of a NifS-like protein from Thermotoga maritima: implications for iron sulfur cluster assembly. J. Mol. Biol. 297:2000;451-464.
27. Mehta P.K., Christen P. The molecular evolution of pyridoxal-5′-phosphate-dependent enzymes. Advan. Enzymol. Relat. Areas Mol. Biol. 74:1998;129-184.
28. McPherson A. Crystallization of Biological Macromolecules. 1999;Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
29. Urbina H.D., Cupp-Vickery J.R., Vickery L.E. Preliminary crystallographic analysis of the cysteine desulfurase IscS from Escherichia coli. Acta Crystallog. sect. D. 58:2002;1224-1225.
30. Brunger A.T., Adams P.D., Clore G.M., Delano W.L., Gros P., Gross-Kunsleve R.W., et al. Crystallography and NMR system (CNS): a new software system for macromolecular structure determination. Acta Crystallog. sect. D. 54:1998;905-921.
31. Matthews B.W. Solvent content of protein crystals. J. Mol. Biol. 33:1968;491-497.
32. Mihara H., Kurihara T., Yoshimura T., Soda K., Esaki N. Cysteine sulfinate desulfinase, a NIFS-like protein of Escherichia coli with selenocysteine lyase and cysteine desulfurase activity. J. Biol. Chem. 272:1997;22417-22424.
33. Fujii T., Maeda M., Mihara H., Kurihara T., Esaki N., Hata Y. Structure of a NifS homolog: X-ray structure analysis of CsdB, an Escherichia coli counterpart of mammalian selenocysteine lyase. Biochemistry. 39:2000;1263-1273.
34. Mihara H., Fujii T., Kato S., Kurihara T., Hata Y., Esaki N. Structure of external aldimine of Escherichia coli CsdB, an Iscs/NifS homolog: implications for its specificity toward selenocysteine. J. Biochem. 131:2002;679-685.
35. Lima C.D. Analysis of the E. coli NifS CsdB protein at 2.0 Å reveals the structural basis for perselenide and persulfide intermediate formation. J. Mol. Biol. 315:2002;1199-1208.
36. Land T., Rouault T.A. Targeting of a human iron-sulfur cluster assembly enzyme, nifs, to different subcellular compartments is regulated through alternative AUG utilization. Mol. Cell. 2:1998;807-815.
37. Leslie, A. G. W. (1998). MOSFLM, 6.0, Cambridge, UK.
38. The CCP4 suite: programs for protein crystallography. Acta Crystallog. sect. D. 50:1994;760-763.
39. Jones T.A. Diffraction methods for biological macromolecules. Interactive computer graphics: FRODO. Methods Enzymol. 115:1985;157-171.
40. Vriend G. WHAT IF - a molecular modeling and drug design program. J. Mol. Graph. 8:1990;52-56.
41. Hutchinson E.G., Thornton J.M. PROMOTIF - a program to identify structural motifs in proteins. Protein Sci. 5:1996;212-220.
42. Laskowski R.A., MacArthur M.W., Moss D.S., Thornton J.M. PROCHECK - a programme to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26:1993;283-291.
43. Evans S.V. SETOR: hardware lighted three-dimensional solid model representations of macromolecules. J. Mol. Graph. 11:1993;134-138.
44. Humphrey W., Dalke A., Schulten K. VMD - visual molecular dynamics. J. Mol. Graph. 14:1996;33-38.