메뉴 건너뛰기




Volumn 8, Issue 7, 1999, Pages 1536-1545

Structural studies by X-ray diffraction on metal substituted desulforedoxin, a rubredoxin-type protein

Author keywords

Crystal structure; Desulfoferrodoxin; Desulforedoxin; Iron sulfur proteins; Metal substitution; Rubredoxin type proteins

Indexed keywords

DESULFOREDOXIN; METALLOPROTEIN; RUBREDOXIN; UNCLASSIFIED DRUG;

EID: 0032805156     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.8.7.1536     Document Type: Article
Times cited : (22)

References (52)
  • 1
    • 0001282755 scopus 로고
    • NH-S hydrogen bonds in Peptococcus aerogenes ferredoxin, Clostridium pasteurianium rubredoxin and Chromatium high potential iron protein
    • Adman ET, Watenpaugh KD, Jensen LH, 1975. NH-S hydrogen bonds in Peptococcus aerogenes ferredoxin, Clostridium pasteurianium rubredoxin and Chromatium high potential iron protein. Proc Natl Acad Sci USA 72:4854-4858.
    • (1975) Proc Natl Acad Sci USA , vol.72 , pp. 4854-4858
    • Adman, E.T.1    Watenpaugh, K.D.2    Jensen, L.H.3
  • 3
    • 0029123025 scopus 로고
    • Crystal structure of desulforedoxin from Desulfovibrio gigas determined at 1.8 Å resolution: A novel non-heme iron protein structure
    • Archer M, Huber R, Tavares P, Moura I, Moura JJG, Carrondo MA, Sieker LC, LeGall J, Romão MJ. 1995. Crystal structure of desulforedoxin from Desulfovibrio gigas determined at 1.8 Å resolution: A novel non-heme iron protein structure. J Mol Biol 257:690-702.
    • (1995) J Mol Biol , vol.257 , pp. 690-702
    • Archer, M.1    Huber, R.2    Tavares, P.3    Moura, I.4    Moura, J.J.G.5    Carrondo, M.A.6    Sieker, L.C.7    LeGall, J.8    Romão, M.J.9
  • 4
    • 0001290698 scopus 로고    scopus 로고
    • The rubredoxin from Clostridium pasteurianum: Mutation of the conserved glycine residues 10 and 43 to alanine and valine
    • Ayhan M, Xiao Z, Lavery MJ, Hamer AM, Nugent KW, Scrofani SDB, Guss M, Wedd AG. 1996. The rubredoxin from Clostridium pasteurianum: Mutation of the conserved glycine residues 10 and 43 to alanine and valine. Inorg Chem 55:5902-5911.
    • (1996) Inorg Chem , vol.55 , pp. 5902-5911
    • Ayhan, M.1    Xiao, Z.2    Lavery, M.J.3    Hamer, A.M.4    Nugent, K.W.5    Scrofani, S.D.B.6    Guss, M.7    Wedd, A.G.8
  • 7
    • 0025695335 scopus 로고
    • The nucleotide sequence of Desulfovibrio gigas desulforedoxin gene indicates that the Desulfovibrio vulgaris rbo gene originated from a gene fusion event
    • Brumlik MJ, LeRoy G, Bruschi M, Voordouw G. 1990. The nucleotide sequence of Desulfovibrio gigas desulforedoxin gene indicates that the Desulfovibrio vulgaris rbo gene originated from a gene fusion event. J Bacteriol 772:7289-7292.
    • (1990) J Bacteriol , vol.772 , pp. 7289-7292
    • Brumlik, M.J.1    LeRoy, G.2    Bruschi, M.3    Voordouw, G.4
  • 8
    • 0024729942 scopus 로고
    • Analysis of the transcriptional unit encoding the genes for rubredoxin (rub) and a putative rubredoxin oxido-reductase (rbo) in Desulfovibrio vulgaris Hildenborough
    • Brumlik MJ, Voordouw G. 1989. Analysis of the transcriptional unit encoding the genes for rubredoxin (rub) and a putative rubredoxin oxido-reductase (rbo) in Desulfovibrio vulgaris Hildenborough. J Bacteriol 171:4996-5004.
    • (1989) J Bacteriol , vol.171 , pp. 4996-5004
    • Brumlik, M.J.1    Voordouw, G.2
  • 10
    • 0000415615 scopus 로고    scopus 로고
    • Coordination sphere versus protein environment as determinants of electronic and functional properties of iron-sulfur proteins
    • Hill HAO, Sadler PJ, Thompson AJ, eds. Berlin, Heidelberg, New York: Springer-Verlag
    • Capozzi F, Ciurli S, Luchinat C. 1998. Coordination sphere versus protein environment as determinants of electronic and functional properties of iron-sulfur proteins. In: Hill HAO, Sadler PJ, Thompson AJ, eds. Structure and bonding - Metal sites in proteins and models - Redox centers. Berlin, Heidelberg, New York: Springer-Verlag, pp 127-160.
    • (1998) Structure and Bonding - Metal Sites in Proteins and Models - Redox Centers , pp. 127-160
    • Capozzi, F.1    Ciurli, S.2    Luchinat, C.3
  • 11
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4. Collaborative Computational Project Number 4. 1994. The CCP4 suite: Programs for protein crystallography. Acta Crystallogr D50:760-763.
    • (1994) Acta Crystallogr , vol.D50 , pp. 760-763
  • 12
    • 0025805918 scopus 로고
    • Crystal structure of a bovine neurophysin II dipeptide complex at 2.8 Å determined from the single wavelength anomalous scattering signal of an incorporated iodine atom
    • Chen LQ, Rose JP, Breslow E, Yang D, Chang WR, Furey WF Jr, Sax M, Wang BC. 1991. Crystal structure of a bovine neurophysin II dipeptide complex at 2.8 Å determined from the single wavelength anomalous scattering signal of an incorporated iodine atom. Proc NatlAcad Sci USA 88:4240-4244.
    • (1991) Proc NatlAcad Sci USA , vol.88 , pp. 4240-4244
    • Chen, L.Q.1    Rose, J.P.2    Breslow, E.3    Yang, D.4    Chang, W.R.5    Furey W.F., Jr.6    Sax, M.7    Wang, B.C.8
  • 14
    • 0029021221 scopus 로고
    • Expression of Desulfovibrio gigas desulforedoxin in Escherichia coli. Purification and characterization of mixed metal isoforms
    • Czaja C, Litwiller R, Tomlinson AJ, Naylor S, Tavares P, LeGall J, Moura JJG, Moura I, Rusnak F. 1995. Expression of Desulfovibrio gigas desulforedoxin in Escherichia coli. Purification and characterization of mixed metal isoforms. J Biol Chem 270:20273-20277.
    • (1995) J Biol Chem , vol.270 , pp. 20273-20277
    • Czaja, C.1    Litwiller, R.2    Tomlinson, A.J.3    Naylor, S.4    Tavares, P.5    LeGall, J.6    Moura, J.J.G.7    Moura, I.8    Rusnak, F.9
  • 15
    • 0029787099 scopus 로고    scopus 로고
    • Zinc- And iron-rubredoxins from Clostridium pasteurianum at atomic resolution: A high precision model of a ZnS4 coordination unit in a protein
    • Dauter Z, Wilson KS, Sieker LC, Moulis JM, Meyer J. 1996. Zinc- and iron-rubredoxins from Clostridium pasteurianum at atomic resolution: A high precision model of a ZnS4 coordination unit in a protein. Proc Natl Acad Sci USA 93:8836-8840.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 8836-8840
    • Dauter, Z.1    Wilson, K.S.2    Sieker, L.C.3    Moulis, J.M.4    Meyer, J.5
  • 16
    • 0029949340 scopus 로고    scopus 로고
    • The structure of Desulfovibrio vulgaris rubrerythrin reveals a unique combination of rubredoxin-like FeS4 and ferritin-like diiron domains
    • deMaré F, Kurtz DM Jr, Nordlund P. 1996. The structure of Desulfovibrio vulgaris rubrerythrin reveals a unique combination of rubredoxin-like FeS4 and ferritin-like diiron domains. Nat Struct Biol 5:539-546.
    • (1996) Nat Struct Biol , vol.5 , pp. 539-546
    • Maré, F.1    Kurtz D.M., Jr.2    Nordlund, P.3
  • 17
    • 0026766750 scopus 로고
    • Expression of a synthetic gene coding for the amino acid sequence of Clostridium pasteurianum rubredoxin
    • Eidsness MK, O Dell SE, Kurtz DM, Robson RL, Scott RA. 1992. Expression of a synthetic gene coding for the amino acid sequence of Clostridium pasteurianum rubredoxin. Protein Eng 5:367-371.
    • (1992) Protein Eng , vol.5 , pp. 367-371
    • Eidsness, M.K.1    O Dell, S.E.2    Kurtz, D.M.3    Robson, R.L.4    Scott, R.A.5
  • 18
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh R, Huber R. 1991. Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallogr A47:392-400.
    • (1991) Acta Crystallogr , vol.A47 , pp. 392-400
    • Engh, R.1    Huber, R.2
  • 19
    • 0030954667 scopus 로고    scopus 로고
    • Studies on the redox centers of the terminal oxidase from Desulfovibrio gigas and evidence for its interaction with rubredoxin
    • Gomes CM, Silva G, Oliveira S, LeGall J, Liu MY, Xavier AV, Rodrigues-Pousada C, Teixeira M. 1997. Studies on the redox centers of the terminal oxidase from Desulfovibrio gigas and evidence for its interaction with rubredoxin. J Biol Chem 272:22502-22508.
    • (1997) J Biol Chem , vol.272 , pp. 22502-22508
    • Gomes, C.M.1    Silva, G.2    Oliveira, S.3    LeGall, J.4    Liu, M.Y.5    Xavier, A.V.6    Rodrigues-Pousada, C.7    Teixeira, M.8
  • 20
  • 21
  • 22
    • 0025104292 scopus 로고
    • Mechanisms of metal ion incorporation into metalloproteins
    • Hausinger RP. 1990. Mechanisms of metal ion incorporation into metalloproteins. Biofactors 2:179-184.
    • (1990) Biofactors , vol.2 , pp. 179-184
    • Hausinger, R.P.1
  • 23
    • 0031744247 scopus 로고    scopus 로고
    • Metal binding to the tetrathiolate motif of desulforedoxin and related polypeptides
    • Kennedy M, Yu L, Lima MJ, Czaja C, Moura I, Moura JJG, Rusnak F. 1998. Metal binding to the tetrathiolate motif of desulforedoxin and related polypeptides. JBIC 3:643-649.
    • (1998) JBIC , vol.3 , pp. 643-649
    • Kennedy, M.1    Yu, L.2    Lima, M.J.3    Czaja, C.4    Moura, I.5    Moura, J.J.G.6    Rusnak, F.7
  • 24
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ. 1991. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J Appl Cryslallogr 24:946-950.
    • (1991) J Appl Cryslallogr , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 25
    • 0017767437 scopus 로고
    • Synthetic analogues of the active sites of iron-sulfur proteins, 14. 1 synthesis, properties, and structures of bis(o-xylyl-α,α′-dithiolato)ferrate(II,III) anions, analogues of oxidized and reduced rubredoxin sites
    • Lane RW, Ibers JA, Frankel RB, Papaefthymiou GC, Holm RH. 1977. Synthetic analogues of the active sites of iron-sulfur proteins, 14. 1 synthesis, properties, and structures of bis(o-xylyl-α,α′-dithiolato)ferrate(II,III) anions, analogues of oxidized and reduced rubredoxin sites. J Am Chem Soc 99:84-98
    • (1977) J Am Chem Soc , vol.99 , pp. 84-98
    • Lane, R.W.1    Ibers, J.A.2    Frankel, R.B.3    Papaefthymiou, G.C.4    Holm, R.H.5
  • 26
    • 0013788501 scopus 로고
    • Rubredoxin: A new electron transfer protein from Clostridium pasteurianum
    • Lovenberg W, Sobel BE. 1965. Rubredoxin: A new electron transfer protein from Clostridium pasteurianum. Proc Nat Acad Sci USA 54:193-199.
    • (1965) Proc Nat Acad Sci USA , vol.54 , pp. 193-199
    • Lovenberg, W.1    Sobel, B.E.2
  • 27
    • 0345396650 scopus 로고
    • Solvent content of protein crystals
    • Matthews BW. 1968. Solvent content of protein crystals. J Mol Biol 245:54-68.
    • (1968) J Mol Biol , vol.245 , pp. 54-68
    • Matthews, B.W.1
  • 28
    • 0028057108 scopus 로고
    • Raster3D version 2.0 - A program for photo-realistic molecular graphics
    • Merritt EA, Murphy MEP. 1994. Raster3D version 2.0 - A program for photo-realistic molecular graphics. Acta Cryslallogr D50:869-873.
    • (1994) Acta Cryslallogr , vol.D50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2
  • 30
    • 0017389657 scopus 로고
    • Isolation and characterization of desulforedoxin, a new type of nonheme iron protein from Desulfovibrio gigas
    • Moura I, Bruschi M. LeGall J, Moura JJG, Xavier AV. 1977. Isolation and characterization of desulforedoxin, a new type of nonheme iron protein from Desulfovibrio gigas. Biochem Biophys Res Commun 75:1037-1044.
    • (1977) Biochem Biophys Res Commun , vol.75 , pp. 1037-1044
    • Moura, I.1    Bruschi, M.2    LeGall, J.3    Moura, J.J.G.4    Xavier, A.V.5
  • 31
    • 77956748167 scopus 로고    scopus 로고
    • Simple and complex iron-sulfur proteins in sulfate reducing bacteria
    • Sikes AG, Cammack RC, eds. Academic Press. In press
    • Moura I, Pereira A, Tavares P, Moura JJG. 1999. Simple and complex iron-sulfur proteins in sulfate reducing bacteria. In: Sikes AG, Cammack RC, eds. Advances in inorganic chemistry. Academic Press. In press.
    • (1999) Advances in Inorganic Chemistry
    • Moura, I.1    Pereira, A.2    Tavares, P.3    Moura, J.J.G.4
  • 32
    • 0028673449 scopus 로고
    • Characterization of three proteins containing multiple iron sites: Rubrerythrin, desulfoferrodoxin, and a protein containing a six-iron cluster
    • Moura I, Tavares P, Ravi N. 1994. Characterization of three proteins containing multiple iron sites: Rubrerythrin, desulfoferrodoxin, and a protein containing a six-iron cluster. Methods Enzymol 243:216-240.
    • (1994) Methods Enzymol , vol.243 , pp. 216-240
    • Moura, I.1    Tavares, P.2    Ravi, N.3
  • 33
    • 0026091738 scopus 로고
    • Spectroscopic studies of cobalt and nickel substituted rubredoxin and desulforedoxin
    • Moura I, Teixeira M, LeGall J, Moura JJG. 1991. Spectroscopic studies of cobalt and nickel substituted rubredoxin and desulforedoxin. J Inorg Biochem 44:127-139.
    • (1991) J Inorg Biochem , vol.44 , pp. 127-139
    • Moura, I.1    Teixeira, M.2    LeGall, J.3    Moura, J.J.G.4
  • 34
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza J. 1994. AMoRe: An automated package for molecular replacement. Acta Crystallogr A50:157-163.
    • (1994) Acta Crystallogr , vol.A50 , pp. 157-163
    • Navaza, J.1
  • 35
    • 0003615263 scopus 로고
    • New Haven, Connecticut: Yale University Press
    • Otwinowski Z, Minor W. 1995. The HKL manual. New Haven, Connecticut: Yale University Press.
    • (1995) The HKL Manual
    • Otwinowski, Z.1    Minor, W.2
  • 36
    • 0014199137 scopus 로고
    • Enzymatic omega-oxidation. II. Function of rubredoxin as the electron carrier in omega-hydroxylation
    • Peterson JA, Kusunose M, Kusunose E, Coon MJ. 1967. Enzymatic omega-oxidation. II. Function of rubredoxin as the electron carrier in omega-hydroxylation. J Biol Chem 242:4334-4340.
    • (1967) J Biol Chem , vol.242 , pp. 4334-4340
    • Peterson, J.A.1    Kusunose, M.2    Kusunose, E.3    Coon, M.J.4
  • 37
    • 0027732943 scopus 로고
    • Analysis, by electrospray ionization mass spectrometry, of several forms of Clostridium pasteurianum rubredoxin
    • Petillot Y, Forest E, Mathieu I, Meyer J, Moulis JM. 1993. Analysis, by electrospray ionization mass spectrometry, of several forms of Clostridium pasteurianum rubredoxin. Biochem J 296:657-661.
    • (1993) Biochem J , vol.296 , pp. 657-661
    • Petillot, Y.1    Forest, E.2    Mathieu, I.3    Meyer, J.4    Moulis, J.M.5
  • 38
    • 0027511224 scopus 로고
    • Nigerythrin and rubrerythrin from Desulfovibrio vulgaris each contain two mononuclear iron centers and two dinuclear iron clusters
    • Pierik AJ, Wolbert RB, Portier GL, Verhagen MF, Hagen WR. 1993. Nigerythrin and rubrerythrin from Desulfovibrio vulgaris each contain two mononuclear iron centers and two dinuclear iron clusters. Eur J Biochem 2/2:237-245.
    • (1993) Eur J Biochem , vol.2 , Issue.2 , pp. 237-245
    • Pierik, A.J.1    Wolbert, R.B.2    Portier, G.L.3    Verhagen, M.F.4    Hagen, W.R.5
  • 41
    • 0030606884 scopus 로고    scopus 로고
    • The cupric geometry of blue copper proteins is not strained
    • Ryde U, Olsson MHM, Pierloot K, Roos BO. 1996. The cupric geometry of blue copper proteins is not strained. J Mol Biol 267:586-596.
    • (1996) J Mol Biol , vol.267 , pp. 586-596
    • Ryde, U.1    Olsson, M.H.M.2    Pierloot, K.3    Roos, B.O.4
  • 45
    • 0019888035 scopus 로고
    • Coupling between oxidation state and hydrogen bond conformation in high potential iron-sulfur protein
    • Sheridan RP, Allen LC, Carter CW Jr. 1981. Coupling between oxidation state and hydrogen bond conformation in high potential iron-sulfur protein. J Biol Chem 256:5052-5057.
    • (1981) J Biol Chem , vol.256 , pp. 5052-5057
    • Sheridan, R.P.1    Allen, L.C.2    Carter C.W., Jr.3
  • 48
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ. 1994. CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22:4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 49
    • 0014251790 scopus 로고
    • Metalloenzymes: The entatic nature of their active sites
    • Vallee BL, Williams RJP. 1968. Metalloenzymes: The entatic nature of their active sites. Proc Natl Acad Sci USA 59:498-505.
    • (1968) Proc Natl Acad Sci USA , vol.59 , pp. 498-505
    • Vallee, B.L.1    Williams, R.J.P.2
  • 51
    • 0028822917 scopus 로고
    • Energized (entatic) states of groups and of secondary structures in proteins and metalloproteins
    • Williams RJP. 1995. Energized (entatic) states of groups and of secondary structures in proteins and metalloproteins. Eur J Biochem 234:363-381.
    • (1995) Eur J Biochem , vol.234 , pp. 363-381
    • Williams, R.J.P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.