Crystal structure of IscA, an iron-sulfur cluster assembly protein from Escherichia coli

Journal of Molecular Biology

Volumn 338, Issue 1, 2004, Pages 127-137

  Cupp Vickery, Jill R ^a   Silberg, Jonathan J ^a,b   Ta, Dennis T ^a   Vickery, Larry E ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b CALIFORNIA INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

Crystal structure; Iron sulfur; IscA; NCS, non crystallographic symmetry; r.m.s., root mean square; SAD, single wavelength anomalous dispersion

Indexed keywords

APOPROTEIN; BACTERIAL PROTEIN; CYSTEINE; IRON DERIVATIVE; METHIONINE DERIVATIVE; MONOMER; PROTEIN ISCA; SELENOMETHIONINE; SULFUR DERIVATIVE; TETRAMER; UNCLASSIFIED DRUG;

ARTICLE; ATOM; CARBOXY TERMINAL SEQUENCE; COMPUTER PROGRAM; CRYSTAL STRUCTURE; ESCHERICHIA COLI; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; PROTEIN STRUCTURE; WAVEFORM;

ESCHERICHIA COLI;

EID: 1842526422     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.02.027     Document Type: Article

References (32)

1. Zheng L., Cash V.L., Flint D.H., Dean D.R. Assembly of iron-sulfur clusters. Identification of an iscSUA-hscBA-fdx gene cluster from Azotobacter vinelandii. J. Biol. Chem. 273:1998;13264-13272.
2. Schwartz C.J., Giel J.L., Patschkowski T., Luther C., Ruzicka F.J., Beinert H., Kiley P. IscR, an Fe-S cluster-containing transcription factor, represses expression of Escherichia coli genes encoding Fe-S cluster assembly proteins. Proc. Natl Acad. Sci. USA. 98:2001;14895-14900.
3. Takahashi Y., Nakamura M. Functional assignment of the ORF2-iscS-iscU-iscA-hscB-hscA-fdx-ORF3 gene cluster involved in the assembly of Fe-S clusters in Escherichia coli. J. Biochem. 126:1999;917-926.
4. Tokumoto U., Takahashi Y. Genetic analysis of the isc operon in Escherichia coli involved in the biogenesis of cellular iron-sulfur proteins. J. Biochem. 130:2001;63-71.
5. Jensen L.T., Culotta V.C. Role of Saccharomyces cerevisiae ISA1 and ISA2 in iron homeostasis. Mol. Cell Biol. 20:2000;3918-3927.
6. Kaut A., Lange H., Diekert K., Kispal G., Lill R. Isa1p is a component of the mitochondria machinery for maturation of cellular iron-sulfur proteins and requires conserved cysteine residues for function. J. Biol. Chem. 275:2000;15955-15961.
7. Pelzer W., Mühlenhoff U., Kiekert K., Siegmund K., Kispal G., Lill R. Mitochondrial Isa2p plays a crucial role in the maturation of cellular iron-sulfur proteins. FEBS Letters. 476:2000;134-139.
8. Ollagnier-de-Choudens S., Mattioli T., Takahasi Y., Fontecave M. Iron-sulfur cluster assembly. Characterization of IscA and evidence for a specific and functional complex with ferredoxin. J. Biol. Chem. 276:2001;22604-22607.
9. Wu G., Mansy S.S., Hemann C., Hille R., Surerus K.K., Cowan J.A. Iron-sulfur cluster biosynthesis: characterization of Schizosaccharomyces pombe Isa1. J. Biol. Inorg. Chem. 7:2002;526-532.
10. 2+ cluster transfer to an apoferredoxin target. Biochemistry. 42:2003;5784-5791.
11. Wollenberg M., Berndt C., Bill E., Schwenn J.D., Seidler A. A dimer of the FeS cluster biosynthesis protein IscA from cyanobacteria binds a [2Fe2S] cluster between two protomers and transfers it to [2Fe2S] and [4Fe4S] apo proteins. Eur. J. Biochem. 270:2003;1662-1671.
12. Krebs C., Agar J.N., Smith A.D., Frazzon J., Dean D.R., Huynh B.H., Johnson M.K. IscA, an alternate scaffold for Fe-S cluster biosynthesis. Biochemistry. 40:2001;14069-14080.
13. Ollagnier-de Choudens S., Nachin L., Snakis Y., Loiseau L., Barras F., Fontecave M. SufA of Erwinia chrysanthemi. Characterization of a scaffold protein required for iron-sulfur cluster assembly. J. Biol. Chem. 278:2003;17993-18001.
14. Agar J.N., Krebs C., Frazzon J., Huynh B.H., Dean D.R., Johnson M.K. IscU as a scaffold for iron-sulfur cluster biosynthesis: sequential assembly of [2Fe-2S] and [4Fe-4S] clusters in IscU. Biochemistry. 39:2000;7856-7862.
15. Nishio K., Nakai M. Transfer of iron-sulfur cluster from NifU to apoferredoxin. J. Biol. Chem. 275:2000;22615-22618.
16. 2+ cluster core in IscU proteins. J. Am. Chem. Soc. 124:2002;8774-8775.
17. Mansy S.S., Wu G., Surerus K.K., Cowan J.A. Iron-sulfur cluster biosynthesis. Thermatoga maritima IscU is a structured iron-sulfur cluster assembly protein. J. Biol. Chem. 277:2002;21397-21404.
18. Wu S., Wu G., Surerus K.K., Cowan J.A. Iron-sulfur cluster biosynthesis. Kinetic analysis of [2Fe-2S] cluster transfer from holo ISU to apo Fd: role of redox chemistry and a conserved aspartate. Biochemistry. 41:2002;8876-8885.
19. Bilder P.W., Ding H., Newcomer M.E. Crystal structure of the ancient. Fe-S scaffold IscA reveals a novel protein fold. Biochemistry. 43:2004;133-139.
20. Matthews B.W. Solvent content of protein crystals. J. Mol. Biol. 33:1968;491-497.
21. 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.
22. Yeh A.P., Ambroggio X.I., Andrade S.L.A., Einsle O., Chatelet C., Meyer J., Rees D.C. High resolution crystal structures of the wild type and cys-55→ser and cys-59→ser variants of the thioredoxin-like [2Fe-2S] ferredoxin from Aquifex aeolicus. J. Biol. Chem. 277:2002;34499-34507.
23. Doublie S. Preparation of selenomethionyl proteins for phase determination. Methods Enzymol. 276:1997;523-530.
24. McPherson A. Crystallization of biological macromolecules. 1999;Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
25. Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallog. sect. D. 50:1994;760-763.
26. 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.
27. Perrakis A., Morris R.J.H., Lamzin V.S. Automated protein model building combined with iterative structure refinement. Nature Struct. Biol. 7:1999;458-463.
28. Jones T.A. Diffraction methods for biological macromolecules. Interactive computer graphics: FRODO. Methods Enzymol. 115:1985;157-171.
29. Terwilliger T.C. Automated main-chain model-building by template - matching and iterative fragment extension. Acta Crystallog. sect. D. 59:2002;34-44.
30. Hutchinson E.G., Thornton J.M. PROMOTIF - a program to identify structural motifs in proteins. Protein Sci. 5:1996;212-220.
31. Evans S.V. SETOR: hardware lighted three-dimensional solid model representations of macromolecules. J. Mol. Graph. 11:1993;134-138.
32. Humphrey W., Dalke A., Schulten K. VMD - visual molecular dynamics. J. Mol. Graph. 14:1996;33-38.