메뉴 건너뛰기




Volumn 290, Issue 4, 1999, Pages 881-902

Crystal structure of the oxidised and reduced acidic cytochrome c3 from Desulfovibrio africanus

Author keywords

Acidic tetraheme cytochrome c3; Crystallisation with Zn and cacodylate; Heme to heme interaction; Multiple anomalous diffraction; Oxidised and reduced crystal structure

Indexed keywords

BACTERIAL PROTEIN; CYTOCHROME C3; HEME; IRON; WATER;

EID: 0032809219     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2917     Document Type: Article
Times cited : (65)

References (73)
  • 1
    • 0032464349 scopus 로고    scopus 로고
    • Analysis of zinc binding sites in protein crystal structures
    • Alberts I. L., Nadassy K., Wodak S. J. Analysis of zinc binding sites in protein crystal structures. Protein Sci. 7:1998;1700-1716.
    • (1998) Protein Sci. , vol.7 , pp. 1700-1716
    • Alberts, I.L.1    Nadassy, K.2    Wodak, S.J.3
  • 2
    • 0030945495 scopus 로고    scopus 로고
    • Incorporating protein conformational flexibility into the calculation of pH-dependent protein properties
    • Alexov E. G., Gunner M. R. Incorporating protein conformational flexibility into the calculation of pH-dependent protein properties. Biophys. J. 74:1997;2075-2093.
    • (1997) Biophys. J. , vol.74 , pp. 2075-2093
    • Alexov, E.G.1    Gunner, M.R.2
  • 3
    • 0014336836 scopus 로고
    • 3 from Desulfovibrio vulgaris (N. C. I. B. 8303)
    • 3 from Desulfovibrio vulgaris (N. C. I. B. 8303). Biochem. J. 109:1968;47P-48P.
    • (1968) Biochem. J. , vol.109
    • Ambler, R.P.1
  • 4
    • 0016122218 scopus 로고
    • Evidence for the periplasmic location of hydrogenase in Desulfovibrio gigas
    • Bell G. R., LeGall J., Peck H. D. Jr. Evidence for the periplasmic location of hydrogenase in Desulfovibrio gigas. J. Bacteriol. 120:1974;994-997.
    • (1974) J. Bacteriol. , vol.120 , pp. 994-997
    • Bell, G.R.1    Legall, J.2    Peck H.D., Jr.3
  • 8
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4
    • CCP4. The CCP4 suite: programs for protein crystallography. Acta Crystallog. sect. D. 50:1994;760-763.
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 760-763
  • 10
    • 0028674194 scopus 로고
    • Tetraheme cytochromes
    • H. D. Jr. Peck, & J. LeGall. London: Academic Press
    • Couthino I. B., Xavier A. V. Tetraheme cytochromes. Peck H. D. Jr, LeGall J. Methods in Enzymology. 1994;119-140 Academic Press, London.
    • (1994) Methods in Enzymology , pp. 119-140
    • Couthino, I.B.1    Xavier, A.V.2
  • 12
    • 0025823103 scopus 로고
    • Dimerization of human growth hormone by zinc
    • Cunningham B. C., Mulkerrin M. G., Wells J. A. Dimerization of human growth hormone by zinc. Science. 253:1991;545-553.
    • (1991) Science , vol.253 , pp. 545-553
    • Cunningham, B.C.1    Mulkerrin, M.G.2    Wells, J.A.3
  • 14
    • 0028007253 scopus 로고
    • Molecular and structural basis of electron transfer in tetra- And octa-heme cytochromes
    • Czjzek M., Payan F., Haser R. Molecular and structural basis of electron transfer in tetra- and octa-heme cytochromes. Biochimie. 76:1994b;546-553.
    • (1994) Biochimie , vol.76 , pp. 546-553
    • Czjzek, M.1    Payan, F.2    Haser, R.3
  • 16
    • 0005384356 scopus 로고
    • The photosynthetic reaction centre from the purple bacterium Rhosopseudomonas viridis
    • Diesenhofer J., Michel H. The photosynthetic reaction centre from the purple bacterium Rhosopseudomonas viridis. EMBO J. 8:1989;2149-2170.
    • (1989) EMBO J. , vol.8 , pp. 2149-2170
    • Diesenhofer, J.1    Michel, H.2
  • 18
    • 0014250081 scopus 로고
    • Pyrrolidonyl peptidase. An enzyme for selective removal of pyrrolidonecarboxylic acid residues from polypeptides
    • Doolittle R. F., Armentrout R. W. Pyrrolidonyl peptidase. An enzyme for selective removal of pyrrolidonecarboxylic acid residues from polypeptides. Biochemistry. 7:1968;516-521.
    • (1968) Biochemistry , vol.7 , pp. 516-521
    • Doolittle, R.F.1    Armentrout, R.W.2
  • 22
    • 0022317258 scopus 로고
    • Direct phase determination based on anomalous scattering
    • H. W. Wyckoff, C. H. W. Hirs, & S. N. Timasheff. London: Academic Press
    • Hendrickson W. A., Smith J. L., Sheriff S. Direct phase determination based on anomalous scattering. Wyckoff H. W., Hirs C. H. W., Timasheff S. N. Methods in Enzymology. 1985;41-55 Academic Press, London.
    • (1985) Methods in Enzymology , pp. 41-55
    • Hendrickson, W.A.1    Smith, J.L.2    Sheriff, S.3
  • 25
    • 0030611275 scopus 로고    scopus 로고
    • The 2.8 Å structure f hydroxylamine oxidoreductase from a nitrifying chemoautotrophic bacterium, Nitrosomonas europaea
    • Igarashi N., Moriyama H., Fujiwara T., Fukumori Y., Tanaka N. The 2.8 Å structure f hydroxylamine oxidoreductase from a nitrifying chemoautotrophic bacterium, Nitrosomonas europaea. Nature Struct. Biol. 4:1997;276-284.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 276-284
    • Igarashi, N.1    Moriyama, H.2    Fujiwara, T.3    Fukumori, Y.4    Tanaka, N.5
  • 26
    • 0001124432 scopus 로고
    • A cytochrome and a green pigment of sulfate-reducing bacteria
    • Ishimoto M., Koyama J., Nagai Y. A cytochrome and a green pigment of sulfate-reducing bacteria. Bull. Chem. Soc. Japan. 27:1954;564-565.
    • (1954) Bull. Chem. Soc. Japan , vol.27 , pp. 564-565
    • Ishimoto, M.1    Koyama, J.2    Nagai, Y.3
  • 27
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T. A., Zou J.-Y., Cowan S. W., Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A. 47:1991;110-119.
    • (1991) Acta Crystallog. Sect. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 28
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallog. 26:1993;795-800.
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 29
    • 0030498233 scopus 로고    scopus 로고
    • XdlMAPMAN and xdlDATAMAN - programs for reformatting, analysis and manipulation of biomacromolecular electron-density maps and reflexions data sets
    • Kleywegt G. J., Jones T. A. xdlMAPMAN and xdlDATAMAN - programs for reformatting, analysis and manipulation of biomacromolecular electron-density maps and reflexions data sets. Acta Crystallog. sect. D. 52:1996;826-828.
    • (1996) Acta Crystallog. Sect. D , vol.52 , pp. 826-828
    • Kleywegt, G.J.1    Jones, T.A.2
  • 30
    • 0000127585 scopus 로고
    • Automated refinement of protein model
    • Lamzin V., Wilson K. Automated refinement of protein model. Acta Crystallog. sect. D. 49:1993;129-147.
    • (1993) Acta Crystallog. Sect. D , vol.49 , pp. 129-147
    • Lamzin, V.1    Wilson, K.2
  • 31
    • 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. Crystallog. 26:1993;283-291.
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 32
    • 0028130331 scopus 로고
    • Localization and specificity of cytochromes and other electron transfer proteins from sulfate-reducing bacteria
    • LeGall J., Payne W. J., Chen L., Liu M. Y., Xavier A. V. Localization and specificity of cytochromes and other electron transfer proteins from sulfate-reducing bacteria. Biochimie. 76:1994;655-665.
    • (1994) Biochimie , vol.76 , pp. 655-665
    • Legall, J.1    Payne, W.J.2    Chen, L.3    Liu, M.Y.4    Xavier, A.V.5
  • 34
    • 0001099937 scopus 로고
    • Traitement statistique des erreurs dans la détermination des structures cristallines
    • Luzzati V. Traitement statistique des erreurs dans la détermination des structures cristallines. Acta Crystallog. 5:1952;802-810.
    • (1952) Acta Crystallog. , vol.5 , pp. 802-810
    • Luzzati, V.1
  • 36
    • 0032544311 scopus 로고    scopus 로고
    • Crystal structures of the catalytic domain of HIV-1 integrase free and complexed with its metal cofactor: High level of similarity of the active site with other viral integrases
    • Maignan S., Guilloteau J.-P., Qing Z.-L., Clément-Mella C., Mikol V. Crystal structures of the catalytic domain of HIV-1 integrase free and complexed with its metal cofactor: high level of similarity of the active site with other viral integrases. J. Mol. Biol. 282:1998;359-368.
    • (1998) J. Mol. Biol. , vol.282 , pp. 359-368
    • Maignan, S.1    Guilloteau, J.-P.2    Qing, Z.-L.3    Clément-Mella, C.4    Mikol, V.5
  • 39
    • 0033081499 scopus 로고    scopus 로고
    • The primary and three-dimensional structures of a nine-haem cytochrome c from Desulfovibrio desulfuricans ATCC 27774 reveal a new member of the Hmc family
    • Matias P. M., Coelho R., Pereira I. A. C., Coelho A. V., Thompson A. W., Sieker L. C., LeGall J., Carrondo M. A. The primary and three-dimensional structures of a nine-haem cytochrome c from Desulfovibrio desulfuricans ATCC 27774 reveal a new member of the Hmc family. Structure. 7:1999;119-130.
    • (1999) Structure , vol.7 , pp. 119-130
    • Matias, P.M.1    Coelho, R.2    Pereira, I.A.C.3    Coelho, A.V.4    Thompson, A.W.5    Sieker, L.C.6    Legall, J.7    Carrondo, M.A.8
  • 40
    • 0017886452 scopus 로고
    • - From equilibrium reactions with flavodoxins, methyl viologen and hydrogen plus hydrogenase
    • - from equilibrium reactions with flavodoxins, methyl viologen and hydrogen plus hydrogenase. Eur. J. Biochem. 85:1978;535-547.
    • (1978) Eur. J. Biochem. , vol.85 , pp. 535-547
    • Mayhew, S.G.1
  • 42
    • 0028838508 scopus 로고
    • Structure of the tetraheme cytochrome from Desulfovibrio desulfuricans ATCC 27774: X-ray diffraction and electron paramagnetic resonance studies
    • Morais J., Palma P. N., Frazão C., Caldeira J., LeGall J., Moura I., Moura J. G., Carrondo M. A. Structure of the tetraheme cytochrome from Desulfovibrio desulfuricans ATCC 27774: X-ray diffraction and electron paramagnetic resonance studies. Biochemistry. 34:1995;12830-12841.
    • (1995) Biochemistry , vol.34 , pp. 12830-12841
    • Morais, J.1    Palma, P.N.2    Frazão, C.3    Caldeira, J.4    Legall, J.5    Moura, I.6    Moura, J.G.7    Carrondo, M.A.8
  • 43
    • 0027372952 scopus 로고
    • Voltammetric studies of the catalytical electron-transfer process between the Desulfovibrio gigas hydrogenase and small proteins isolated from the same genus
    • Moreno C., Franco R., Moura I., LeGall J., Moura J. J. G. Voltammetric studies of the catalytical electron-transfer process between the Desulfovibrio gigas hydrogenase and small proteins isolated from the same genus. Eur. J. Biochem. 217:1993;981-989.
    • (1993) Eur. J. Biochem. , vol.217 , pp. 981-989
    • Moreno, C.1    Franco, R.2    Moura, I.3    Legall, J.4    Moura, J.J.G.5
  • 44
    • 0025907366 scopus 로고
    • Structural and functional approach toward a classification of the complex cytochrome c system found in sulphate-reducing bacteria
    • Moura J. J. G., Costa C., Liu M. Y., Moura I., LeGall J. Structural and functional approach toward a classification of the complex cytochrome c system found in sulphate-reducing bacteria. Biochim. Biophys. Acta. 1058:1991;61-66.
    • (1991) Biochim. Biophys. Acta , vol.1058 , pp. 61-66
    • Moura, J.J.G.1    Costa, C.2    Liu, M.Y.3    Moura, I.4    Legall, J.5
  • 45
    • 0028497464 scopus 로고
    • A 200 mm input field, 5-80 keV detector based on an X-ray image intensifier and CCD camera
    • Moy J. P. A 200 mm input field, 5-80 keV detector based on an X-ray image intensifier and CCD camera. Nucl. Instrum. Methods sect. A. 348:1994;641-644.
    • (1994) Nucl. Instrum. Methods Sect. a , vol.348 , pp. 641-644
    • Moy, J.P.1
  • 47
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza J. AMoRe: an automated package for molecular replacement. Acta Crystallog. sect. A. 50:1994;157-163.
    • (1994) Acta Crystallog. Sect. a , vol.50 , pp. 157-163
    • Navaza, J.1
  • 48
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K. A., Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins: Struct. Funct. Genet. 11:1991;281-296.
    • (1991) Proteins: Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 51
    • 0019385304 scopus 로고
    • Localization of dehydrogenases, reductases, and electron transfer components in the sulphate-reducing bacterium Desulfovibrio gigas
    • Odom J. M., Peck H. D. Jr. Localization of dehydrogenases, reductases, and electron transfer components in the sulphate-reducing bacterium Desulfovibrio gigas. J. Bacteriol. 147:1981;161-169.
    • (1981) J. Bacteriol. , vol.147 , pp. 161-169
    • Odom, J.M.1    Peck H.D., Jr.2
  • 53
    • 0029645282 scopus 로고
    • Crystal structure of the superantigen enterotoxin C2 from Staphylococcus aureus reveals a zinc-binding site
    • Papageorgiou A. C., Acharya K. R., Shapiro R., Passalacqua E. F., Brehm R. D., Tranter H. Crystal structure of the superantigen enterotoxin C2 from Staphylococcus aureus reveals a zinc-binding site. Structure. 3:1995;769-779.
    • (1995) Structure , vol.3 , pp. 769-779
    • Papageorgiou, A.C.1    Acharya, K.R.2    Shapiro, R.3    Passalacqua, E.F.4    Brehm, R.D.5    Tranter, H.6
  • 55
    • 0027056273 scopus 로고
    • Crystal structure of a complex between electron transfer partners, cytochrome c peroxidase and cytochrome c
    • Pelletier H., Kraut J. Crystal structure of a complex between electron transfer partners, cytochrome c peroxidase and cytochrome c. Science. 258:1992;1748-1755.
    • (1992) Science , vol.258 , pp. 1748-1755
    • Pelletier, H.1    Kraut, J.2
  • 59
    • 0027970990 scopus 로고
    • Molecular biology of c-type cytochromes from Desulfovibrio vulgaris Hildenborough
    • Pollock W. B. R., Voordouw G. Molecular biology of c-type cytochromes from Desulfovibrio vulgaris Hildenborough. Biochimie. 76:1994;554-560.
    • (1994) Biochimie , vol.76 , pp. 554-560
    • Pollock, W.B.R.1    Voordouw, G.2
  • 60
    • 0002100783 scopus 로고
    • Presence of cytochrome in an obligate anaerobe
    • Postgate J. R. Presence of cytochrome in an obligate anaerobe. Biochem. J. 56:1954.
    • (1954) Biochem. J. , vol.56
    • Postgate, J.R.1
  • 62
    • 0017282573 scopus 로고
    • An hypothetical structure for an intermolecular electron transfer complex of cytochromes c and b
    • Salemme F. R. An hypothetical structure for an intermolecular electron transfer complex of cytochromes c and b. J. Mol. Biol. 102:1976;563-568.
    • (1976) J. Mol. Biol. , vol.102 , pp. 563-568
    • Salemme, F.R.1
  • 63
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A., Blundell T. L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234:1993;779-815.
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 66
    • 0031045587 scopus 로고    scopus 로고
    • Patterson superposition and ab Initio phasing
    • C. W. Jr. Carter, & R. M. Sweet. London: Academic Press
    • Sheldrick G. M. Patterson superposition and ab Initio phasing. Carter C. W. Jr, Sweet R. M. Methods in Enzymology. 1997;628-641 Academic Press, London.
    • (1997) Methods in Enzymology , pp. 628-641
    • Sheldrick, G.M.1
  • 70
    • 0030862401 scopus 로고    scopus 로고
    • Structure of cytochrome c′ from Rhodobacter capsulatus strain St Louis: An unusual molecular association induced by bridging Zn ions
    • Tahirov T. H., Misaki S., Meyer T. E., Cusanovich M. A., Higuchi Y., Yasuoka N. Structure of cytochrome c′ from Rhodobacter capsulatus strain St Louis: an unusual molecular association induced by bridging Zn ions. Acta Crystallog. sect. D. 53:1997;658-664.
    • (1997) Acta Crystallog. Sect. D , vol.53 , pp. 658-664
    • Tahirov, T.H.1    Misaki, S.2    Meyer, T.E.3    Cusanovich, M.A.4    Higuchi, Y.5    Yasuoka, N.6
  • 73
    • 0021722670 scopus 로고
    • 3 catalyzed by hydrogenase with hydrogen
    • 3 catalyzed by hydrogenase with hydrogen. Biochim. Biophys. Acta. 767:1984;288-294.
    • (1984) Biochim. Biophys. Acta , vol.767 , pp. 288-294
    • Yagi, T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.