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Volumn 27, Issue 4, 1997, Pages 517-522

Structure prediction and fold recognition for the ferrochelatase family of proteins

Author keywords

barrel; Bacillus subtilis; ferrochelatase; hemH; protein structure prediction

Indexed keywords

FERROCHELATASE; IRON; PROTOPORPHYRIN;

EID: 0030920605     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(199704)27:4<517::AID-PROT5>3.0.CO;2-7     Document Type: Article
Times cited : (5)

References (18)
  • 1
    • 0001979473 scopus 로고
    • Conversion of coproporphyrinogen to protoheme in higher eukaryotes and bacteria: Terminal three enzymes
    • Dailey, H.A. (ed.). New York: McGraw-Hill
    • Dailey, H.A. Conversion of coproporphyrinogen to protoheme in higher eukaryotes and bacteria: Terminal three enzymes. In: "Biosynthesis of Heme and Chlorophyll." Dailey, H.A. (ed.). New York: McGraw-Hill, 1990:123-161.
    • (1990) Biosynthesis of Heme and Chlorophyll , pp. 123-161
    • Dailey, H.A.1
  • 2
    • 0024378380 scopus 로고
    • Interaction of porphyrins and metalloporphyrins with mouse ferrochelatase: A model for the active site ferrochelatase
    • Dailey, H.A., Jones, C.S., Karr, S.W. Interaction of porphyrins and metalloporphyrins with mouse ferrochelatase: A model for the active site ferrochelatase. Biochim. Biophys. Acta 999:7-11, 1989.
    • (1989) Biochim. Biophys. Acta , vol.999 , pp. 7-11
    • Dailey, H.A.1    Jones, C.S.2    Karr, S.W.3
  • 3
    • 0028029512 scopus 로고
    • Site-directed mutagenesis of human ferrochelatase: Identification of histidine-263 as a binding site for metal ions
    • Kohno, H., Okuda, M. Furukawa, T., Tokunaga, R., Taketani, S. Site-directed mutagenesis of human ferrochelatase: Identification of histidine-263 as a binding site for metal ions. Biochim. Biophys. Acta 1209:95-100, 1994.
    • (1994) Biochim. Biophys. Acta , vol.1209 , pp. 95-100
    • Kohno, H.1    Okuda, M.2    Furukawa, T.3    Tokunaga, R.4    Taketani, S.5
  • 4
    • 0029586760 scopus 로고
    • Purification, crystallization, and preliminary X-ray analysis of Bacillus subtilis ferrochelatase
    • Hansson, M., Al-Karadaghi, S. Purification, crystallization, and preliminary X-ray analysis of Bacillus subtilis ferrochelatase. Proteins 23:607-609, 1995.
    • (1995) Proteins , vol.23 , pp. 607-609
    • Hansson, M.1    Al-Karadaghi, S.2
  • 5
    • 0030052366 scopus 로고    scopus 로고
    • Protein fold recognition by sequence threading: Tools and assessment techniques
    • Miller, R.T., Jones, D.T., Thornton, J.M. Protein fold recognition by sequence threading: Tools and assessment techniques. FASEB J. 10:171-178, 1996.
    • (1996) FASEB J. , vol.10 , pp. 171-178
    • Miller, R.T.1    Jones, D.T.2    Thornton, J.M.3
  • 6
    • 0028865588 scopus 로고
    • Successful protein fold recognition by optimal sequence threading validated by rigorous blind testing
    • Jones, D.T., Miller, R.T., Thornton, J.M. Successful protein fold recognition by optimal sequence threading validated by rigorous blind testing. Proteins Struct. Funct. Genet. 23:387-397, 1995.
    • (1995) Proteins Struct. Funct. Genet. , vol.23 , pp. 387-397
    • Jones, D.T.1    Miller, R.T.2    Thornton, J.M.3
  • 8
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S., Thornton, J.M. PROCHECK: A program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26:283-291, 1993.
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 9
    • 0026676696 scopus 로고
    • Cloning and characterization of the Bacillus subtilis hemEHY gene cluster, which encodes protoheme IX biosynthetic enzymes
    • Hansson, M., Hederstedt, L. Cloning and characterization of the Bacillus subtilis hemEHY gene cluster, which encodes protoheme IX biosynthetic enzymes. J. Bacteriol. 174:8081-8093, 1992.
    • (1992) J. Bacteriol. , vol.174 , pp. 8081-8093
    • Hansson, M.1    Hederstedt, L.2
  • 10
    • 0028147501 scopus 로고
    • Purification and characterisation of a water-soluble ferrochelatase from Bacillus subtilis
    • Hansson, M., Hederstedt, L. Purification and characterisation of a water-soluble ferrochelatase from Bacillus subtilis. Eur. J. Biochem. 220:201-208, 1994.
    • (1994) Eur. J. Biochem. , vol.220 , pp. 201-208
    • Hansson, M.1    Hederstedt, L.2
  • 11
    • 0003648101 scopus 로고
    • Madison, WI: September
    • Program Manual for the Wisconsin Package, Version 8, Madison, WI: September 1994; Program Manual for the EGCG Package, Peter Rice, Cambridge, UK: The Sanger Centre, Hinxton Hall, August 1995.
    • (1994) Program Manual for the Wisconsin Package, Version 8
  • 12
    • 0003648112 scopus 로고
    • Peter Rice, Cambridge, UK: The Sanger Centre, Hinxton Hall, August
    • Program Manual for the Wisconsin Package, Version 8, Madison, WI: September 1994; Program Manual for the EGCG Package, Peter Rice, Cambridge, UK: The Sanger Centre, Hinxton Hall, August 1995.
    • (1995) Program Manual for the EGCG Package
  • 13
    • 0028033747 scopus 로고
    • A proposed structure for the 'family 18' chitinases: A possible function for narbonin
    • Coulson, A.F. A proposed structure for the 'family 18' chitinases: A possible function for narbonin. FEBS Lett. 354:41-44, 1994.
    • (1994) FEBS Lett. , vol.354 , pp. 41-44
    • Coulson, A.F.1
  • 14
    • 0029889988 scopus 로고    scopus 로고
    • Predicting one-dimensional protein structure by profile-based neural networks
    • Rost, B. Predicting one-dimensional protein structure by profile-based neural networks. Methods Enzymol. 266:525-539, 1996.
    • (1996) Methods Enzymol. , vol.266 , pp. 525-539
    • Rost, B.1
  • 15
    • 0030052366 scopus 로고    scopus 로고
    • Protein fold recognition by sequence threading: Tools and assessment techniques
    • Miller, R.T., Jones, D.T., Thornton, J.M. Protein fold recognition by sequence threading: Tools and assessment techniques. FASEB J. 10:171-178, 1996.
    • (1996) FASEB J. , vol.10 , pp. 171-178
    • Miller, R.T.1    Jones, D.T.2    Thornton, J.M.3
  • 16
    • 0025284257 scopus 로고
    • The evolution of α/β barrel enzymes
    • Farber, G.K., Petsko, G.A. The evolution of α/β barrel enzymes. TIBS 15:228-234, 1990.
    • (1990) TIBS , vol.15 , pp. 228-234
    • Farber, G.K.1    Petsko, G.A.2
  • 17
    • 0029974210 scopus 로고    scopus 로고
    • Probing the active-site residues in Saccharomyces cerevisiae ferrochelatase by directed mutagenesis
    • Gora, M., Grzybowska, E., Rytka, J., Labbe-Bois, R. Probing the active-site residues in Saccharomyces cerevisiae ferrochelatase by directed mutagenesis. J. Biol. Chem. 271:11810-11816, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11810-11816
    • Gora, M.1    Grzybowska, E.2    Rytka, J.3    Labbe-Bois, R.4
  • 18
    • 0002005074 scopus 로고
    • Ferrochelatase in Saccharomyces cersvisiae
    • Winkelmann, G., Winge, D.R. (eds.). New York: Marcel Dekker
    • Labbe-Bois, R., Camadro, J.-M. Ferrochelatase in Saccharomyces cersvisiae. In: "Metal Ions in Fungi". Winkelmann, G., Winge, D.R. (eds.). New York: Marcel Dekker, 1994:413-453.
    • (1994) Metal Ions in Fungi , pp. 413-453
    • Labbe-Bois, R.1    Camadro, J.-M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.