Crystal structure of ferrochelatase: The terminal enzyme in heme biosynthesis

Structure

Volumn 5, Issue 11, 1997, Pages 1501-1510

  Al Karadaghi, Salam ^a   Hansson, Mats ^b   Nikonov, Stanislav ^a,c   Jönsson, Bodil ^a   Hederstedt, Lars ^a  

^a LUND UNIVERSITY   (Sweden)

^b CARLSBERG LABORATORY   (Denmark)

^c INSTITUTE OF PROTEIN RESEARCH   (Russian Federation)

Author keywords

Bacillus subtilis; Ferrochelatase structure; Heme synthesis; Porphyrin metallation

Indexed keywords

EID: 0031573454     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(97)00299-2     Document Type: Article

References (33)

1. Ferreira, G.C. (1995). Heme biosynthesis: biochemistry, molecular biology, and relationship to disease. J. Bioeng. Biomembr. 27, 147-150.
2. Labbe-Bois, R. & Camadro, J.-M. (1994). Ferrochelatase in Saccharomyces cerevisiae. In Metal Ions in Fungi. (Winkelman, G. & Winge, D.R., eds), pp. 413-453, Marcel Dekker Inc., New York, NY.
3. Hansson, M. & Hederstedt, L. (1994). Purification and characterisation of a water-soluble ferrochelatase from Bacillus subtilis. Eur. J. Biochem. 220, 201-208.
4. Ferreira, G.G., Franco, R., Lloyd, S.G., Moura, I., Moura, J.J.G. & Huynh, B.H. (1995). Structure and function of ferrochelatase. J. Bioenerg. Biomembr. 27, 221-229.
5. Kohno, H., Okuda, M., Furukawa, T., Tokunaga, R. & Taketani, S. (1994). Site-directed mutagenesis of human ferrochelatase: identification of histidine-263 as a binding site for metal ions. Biochim. Biophys. Acta 1209, 95-100.
6. Gora, M., Grzybowska, E., Rytka, J. & Labbe-Bois, R. (1996). Probing the active-site residues in Saccharomyces cerevisiae ferrochelatase by directed mutagenesis. J. Biol. Chem. 271, 11810-11816.
7. Lamoril, J., Boulechfar, S., de Verneuil, H., Grandchamp, B., Nordamnn, Y. & Deybach, J.-C. (1991). Human erythropoietic protoporphyria: two point mutations in the ferrochelatase gene. Biochem. Biophys. Res. Commun. 181, 594-599.
8. Hambright, P. & Chock, P.B. (1974). Metal-porphyrin interactions. III. A dissociative-interchange mechanism for metal ion incorporation into porphyrin molecules. J. Am. Chem. Soc. 96, 3123-3131.
9. Lavallee, D.K. (1988). Porphyrin metallation reactions in biochemistry. Mol. Struct. Energ. 9, 279-314.
10. Hansson, M. & Hederstedt, L. (1992). Cloning and characterization of the Bacillus subtilis hemEHY gene cluster, which encodes protoheme IX biosynthetic enzymes. J. Bacteriol. 174, 8081-8093.
11. Kabsch, W. & Sander, C. (1983). Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical feature. Biopolymers 22, 2577-2637.
12. Holm, L. & Sander, C. (1993). Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233, 123-138.
13. Quiocho, F.A. & Vyas, N.K. (1984). Novel stereospecificity of L-arabinose binding protein. Nature 310, 381-386.
14. Ferreira, G.C., etal., & Huynh, B.H. (1994). Mammalian ferrochelatase, a new addition to the metaloenzyme family. J. Biol. Chem. 269, 7062-7065.
15. Dailey, H.A., Finnegan, M.G. & Johnson, M.K. (1994). Human ferrochelatase is an iron-sulfur protein. Biochemistry 33, 403-407.
16. Jensen, P.E., Gibson, L.C.D., Henningsen, K.W. & Hunter, C.N. (1997). Expression of the ch/I, ch/D, and ch/H genes from the cyanobacterium Synechocystis PCC6803 in Escherichia coli and demonstration that the three cognate proteins are required for magnesium-protoporphyrin chelatase. J. Biol. Chem. 271, 16662-16667.
17. Dailey, H.A., Cheryl, S.J. & Karr, S.W. (1989). Interaction of free porphyrins with mouse ferrochelatase. A model for the active site of ferrochelatase. Biochim. Biophys. Acta 999, 7-11.
18. Dailey, H.A. & Fleming, J.E. (1986). The role of arginyl residues in porphyrin binding to ferrochelatase. J. Biol. Chem. 261, 7902-7905.
19. Flocco, M.M. & Mowbray, S.L. (1994). The 1.9 Å X-ray structure of a closed unliganded form of the periplasmic glucose/galactose receptor from Salmonella typhimurium. J. Biol. Chem. 269, 8931-8936.
20. Hansson, M. & AI-Karadaghi, S. (1995). Purification, crystallization, and preliminary X-ray analysis of Bacillus subtilis ferrochelatase. Proteins 23, 607-609.
21. Otwinowski, Z. & Minor, W. (1996). Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-325.
22. Taketani, S. & Tokunaga, R. (1981). Rat liver ferrochelatase. J. Biol. Chem. 256, 12748-12753.
23. Dailey, H.A. (1987). Metal inhibition of ferrochelatase. Annu. NY Acad. Sci. 514, 81-86.
24. Collaborative Computational Project, Number 4. (1994). The CCP4 suite: programs for protein crystallography. Acta Cryst. D 50, 760-763.
25. Cowtan, K. (1994). 'dm': an automated procedure for phase improvement by density modification. In Joint CCP4 and ESF-EACBM Newsletter on Protein Crystallography. 31, 34-38.
26. Jones, T.A., Zou, J.-Y., Cowan, S.W. & Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Cryst. A 47, 110-119.
27. Read, R.J. (1986). Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Cryst. A 42, 140-149.
28. 1 ATPase. Acta Cryst. D 52, 30-42.
29. Brünger, AT. (1990). X-PLOR Version 3.1, a System for X-ray Crystallography and NMR. Yale University Press, New Haven, CT.
30. Kleywegt, G.J. & Jones, T.A. (1996). xdlMAPMAN and xdlDATAMAN - programs for reformatting, analysis and manipulation of biomacromolecular electron-density maps and reflection data sets. Acta Cryst. D 52, 826-828.
31. Laskowski, R.A., MacArthur, M.V., Moss, D.S. & Thornton, J.M. (1993). PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26, 283-291.
32. Kraulis, P. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24, 946-950.
33. Nicholls, A., Sharp, K. & Honig, B. (1991). Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-296.