The Asymmetric IscA Homodimer with an Exposed [2Fe-2S] Cluster Suggests the Structural Basis of the Fe-S Cluster Biosynthetic Scaffold

Journal of Molecular Biology

Volumn 360, Issue 1, 2006, Pages 117-132

  Morimoto, Kozo ^a   Yamashita, Eiki ^a   Kondou, Youhei ^a   Lee, Soo Jae ^a   Arisaka, Fumio ^b   Tsukihara, Tomitake ^a   Nakai, Masato ^a  

^a OSAKA UNIVERSITY   (Japan)

^b TOKYO INSTITUTE OF TECHNOLOGY   (Japan)

Author keywords

biosynthesis; iron sulfur cluster; IscA; metallo cofactor; molecular scaffold

Indexed keywords

CYSTEINE; IRON SULFUR PROTEIN; PROTEIN ISCA; SCAFFOLD PROTEIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BIOCHEMISTRY; BIOSYNTHESIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; CYANOBACTERIUM; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN STABILITY; THERMOSYNECHOCOCCUS ELONGATUS;

THERMOSYNECHOCOCCUS ELONGATUS;

EID: 33745271510     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.04.067     Document Type: Article

References (38)

1. Matsubara H., and Saeki K. Structural and functional diversity of ferredoxins and related proteins. Advan. Inorg. Chem. 38 (1992) 223-284
2. Beinert H. Iron-sulfur proteins: ancient structures, still full of surprises. J. Biol. Inorg. Chem. 5 (2000) 2-15
3. Rouault T.A., and Tong W.-H. Iron-sulphur cluster biogenesis and mitochondrial iron homeostasis. Nature Rev. Mol. Cell Biol. 6 (2005) 345-351
4. Frazzon J., and Dean D.R. Formation of iron-sulfur clusters in bacteria. Curr. Opin. Chem. Biol. 7 (2003) 166-173
5. Muhlenhoff U., and Lill R. Biogenesis of iron-sulfur proteins in eukaryotes. Biochim. Biophys. Acta 1459 (2000) 370-382
6. Nakai M., Nishio K., Morimoto K., Yabe T., and Kikuchi S. Molecular scaffolds involved in iron-sulfur cluster biosynthesis. In: Pandalai S.G. (Ed). Recent Research Developments in Proteins (2002), Transworld Research Network, Tricandrum, India 1-11
7. Yuvaniyama P., Agar J.N., Cash V.L., Johnson M.K., and 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
8. Nishio K., and Nakai M. Transfer of iron-sulfur cluster from NifU to apoferredoxin. J. Biol. Chem. 275 (2000) 22615-22618
9. Agar J.N., Krebs C., Frazzon J., Huynh B.H., Dean D.R., and Johnson M.K. IscU as a scaffold for iron-sulfur cluster biosynthesis: sequential assembly of [2Fe-2S] and [4Fe-4S] cluster in IscU. Biochemistry 39 (2000) 7856-7862
10. Krebs C., Agar J.N., Smith A.D., Frazzon J., Dean D.R., Huynh B.H., and Johnson M.K. IscA, an alternate scaffold for Fe-S cluster biosynthesis. Biochemistry 40 (2001) 14069-14080
11. Yabe T., Morimoto K., Kikuchi S., Nishio K., Terashima I., and Nakai M. The Arabidopsis chloroplastic NifU-like protein CnfU, which can act as a iron-sulfur cluster scaffold protein, is required for biogenesis of ferredoxin and photosystem I. Plant Cell 16 (2004) 993-1007
12. Ollagnier-de-Choudens S., Mattioli T., Takahashi Y., and 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
13. Jensen L.T., and Culotta V.C. Role of Saccharonyces cerevisiae ISA1 and ISA2 in iron homeostasis. Mol. Cell Biol. 20 (2000) 3918-3927
14. Pelzer W., Mühlenhoff U., Diekert K., Siegmund K., Kispal G., and Lill R. Mitochondrial Isa2p plays a crucial role in the maturation of cellular iron-sulfur proteins. FEBS Letters 476 (2000) 134-139
15. Ding H., Clark R.J., and Ding B. IscA mediates iron delivery for assembly of iron-sulfur clusters in IscU under the limited accessible free iron conditions. J. Biol. Chem. 279 (2004) 37499-37504
16. Morimoto K., and Nakai M. Identification of a novel prokaryotic HEAT-repeats-containing protein which interacts with a cyanobacterial IscA homolog. FEBS Letters 519 (2002) 123-127
17. Wollenberg M., Berndt C., Bill E., Schwenn J.D., and Seidler A. A dimer of the Fe-S cluster biosynthesis protein IscA from cyanobacteria binds a [2Fe2S] cluster between two subunits and transfers it to [2Fe2S] and [4Fe4S] apo proteins. Eur. J. Biochem. 270 (2003) 1662-1671
18. Wu G., Mansy S.S., Hemann C., Hille R., Surerus K.K., and Cowan J.A. Iron-sulfur cluster biosynthesis: characterization of Schizosaccharomyces pombe Isa1. J. Biol. Inorg. Chem. 7 (2002) 526-532
19. Yabe T., and Nakai M. Arabidopsis AtIscA-I is affected by deficiency of Fe-S cluster biosynthetic scaffold AtCnfU-V. Biochem. Biophys. Res. Commun. 340 (2006) 1047-1052
20. Ollagnier-de-Choudens S., Sanakis Y., and Fontecave M. SufA/IscA: reactivity studies of a class of scaffold proteins involved in [Fe-S] cluster assembly. J. Biol. Inorg. Chem. 9 (2004) 828-838
21. Abdel-Ghany S.E., Ye H., Garifullina G.F., Zhang L., Pilon-Smits E.A., and Pilon M. Iron-sulfur cluster biosynthesis in chloroplasts. Involvement of the scaffold protein CpIscA. Plant Physiol. 138 (2005) 161-172
22. Bilder P., Ding H., and Newcomer M. Crystal structure of the ancient, Fe-S scaffold IscA reveals a novel protein fold. Biochemistry 43 (2004) 133-139
23. Cupp-Vickery J.R., Silberg J.J., Ta D.T., and Vickery L.E. Crystal structure of IscA, an iron-sulfur cluster assembly protein from Escherichia coli. J. Mol. Biol. 338 (2004) 127-137
24. Xu D., Liu G., Xiao R., Acton T., Goldsmith-Fischman S., Honig B., et al. NMR structure of the hypothetical protein AQ-1857 encoded by the Y157 gene from Aquifex aeolicus reveals a novel protein fold. Proteins: Struct. Funct. Genet. 54 (2004) 794-796
25. Morimoto K., Sato S., Tabata S., and Nakai M. A HEAT-repeats containing protein, IaiH, stabilizes the iron-sulfur cluster bound to the cyanobacterial IscA homolog, IscA2. J. Biochem. 134 (2003) 211-217
26. Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S., et al. Complete genome structure of the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1. DNA Res. 9 (2002) 123-130
27. Liu Y., and Eisenberg D. 3D domain swapping: as domains continue to swap. Protein Sci. 11 (2000) 1285-1299
28. Matthews B.W. Solvent content of protein crystals. J. Mol. Biol. 33 (1968) 491-497
29. Tsukihara T., Fukuyama K., Tahara H., Katsube Y., Matsuura Y., Tanaka N., et al. X-ray analysis of ferredoxin from Spirulina platensis. II. Chelate structure of active center. J. Biochem. 84 (1978) 1645-1647
30. Otwinowski Z., and Minor W. Processing of x-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
31. CCP4 (Collaborative Computational Project, Number 4). The CCP4 suite: programs for protein crystallography. Acta Crystallog. sect. D 50 (1994) 760-763
32. Terwilliger T.C. Maximum-likelihood density modification. Acta Crystallog. sect. D 56 (2000) 965-972
33. Jones T.A., Zou J.Y., Cowan S.W., and Kjeldgaard M. Improved methods for building models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A 47 (1991) 110-119
34. Murshudov G.V., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by maximum-likelihood method. Acta Crystallog. sect. D 53 (1997) 240-255
35. Brünger A.T., Adams P.D., Clore G.M., DeLano W.L., Gros P., Grosse-Kunstleve R.W., et al. Crystallography and NMR system: a new software suite for macromolecular structure determination. Acta Crystallog. sect. D 54 (1998) 905-921
36. Koradi R., Billeter M., and Wüthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14 (1996) 51-55
37. Schuck P. Size distribution of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling. Biophys. J. 78 (2000) 1606-1619
38. Wada K., Hasegawa Y., Gong Z., Minami Y., Fukuyama K., and Takahashi Y. Crystal structure of Escherichia coli SufA involved in biosynthesis of iron-sulfur clusters: implications for a functional dimer. FEBS Letters 579 (2005) 6543-6548