메뉴 건너뛰기




Volumn 7, Issue 4, 1998, Pages 928-937

NMR determination of the global structure of the 113Cd derivative of desulforedoxin: Investigation of the hydrogen bonding pattern at the metal center

Author keywords

3D structure; 113Cd; Desulforedoxin; NMR; Rubredoxin type proteins

Indexed keywords

METALLOPROTEIN; RUBREDOXIN; ZINC FINGER PROTEIN;

EID: 0031978742     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560070410     Document Type: Article
Times cited : (24)

References (25)
  • 1
    • 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, Sicker 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 251:690-702.
    • (1995) J Mol Biol , vol.251 , pp. 690-702
    • Archer, M.1    Huber, R.2    Tavares, P.3    Moura, I.4    Moura, J.J.G.5    Carrondo, M.A.6    Sicker, L.C.7    LeGall, J.8    Romão, M.J.9
  • 2
    • 0002303151 scopus 로고
    • 113Cd NMR to biological systems
    • Berliner LJ, Reuben J, eds. New York: Plenum Publishing Corporation
    • 113Cd NMR to biological systems. In: Berliner LJ, Reuben J, eds. Biological magnetic resonance. New York: Plenum Publishing Corporation. pp 79-144.
    • (1982) Biological Magnetic Resonance , pp. 79-144
    • Armitage, I.M.1    Otvos, J.D.2
  • 3
    • 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 35:5902-5911.
    • (1996) Inorg Chem , vol.35 , 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
  • 4
    • 0028004661 scopus 로고
    • The three-dimensional structure in solution of the paramagnetic high-potential iron-sulfur protein I from Ectothiorrhodospira halophila through nuclear magnetic resonance
    • Banci L, Bertini I, Eltis LD, Felli IC, Kastrau DH, Luchinat C, Piccioli M, Pierattelli R, Smith M. 1994. The three-dimensional structure in solution of the paramagnetic high-potential iron-sulfur protein I from Ectothiorrhodospira halophila through nuclear magnetic resonance. Eur J Biochem 225:715-725.
    • (1994) Eur J Biochem , vol.225 , pp. 715-725
    • Banci, L.1    Bertini, I.2    Eltis, L.D.3    Felli, I.C.4    Kastrau, D.H.5    Luchinat, C.6    Piccioli, M.7    Pierattelli, R.8    Smith, M.9
  • 5
    • 0343459675 scopus 로고
    • The program XEASY for computer-supported NMR spectral analysis of biological macromolecules
    • Bartels Ch, Xia TH, Billiter M, Güntert P, Wüthrich K. 1995. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. J Biolmol NMR 5:1-10.
    • (1995) J Biolmol NMR , vol.5 , pp. 1-10
    • Bartels, Ch.1    Xia, T.H.2    Billiter, M.3    Güntert, P.4    Wüthrich, K.5
  • 8
    • 0019889444 scopus 로고
    • Combined use of proton-proton Overhauser enhancements and a distance geometry algorithm for determination of polypeptide conformations: Application to micelle-bound glucagon
    • Braun W, Bösch C, Brown LR, Gõ N, Wüthrich K. 1981. Combined use of proton-proton Overhauser enhancements and a distance geometry algorithm for determination of polypeptide conformations: Application to micelle-bound glucagon. Biochim Biophys Acta 667:377-396.
    • (1981) Biochim Biophys Acta , vol.667 , pp. 377-396
    • Braun, W.1    Bösch, C.2    Brown, L.R.3    Gõ, N.4    Wüthrich, K.5
  • 9
    • 0018672686 scopus 로고
    • The amino acid sequence of desulforedoxin, a new type of non-heme iron protein from Desulfovibrio gigas
    • Bruschi M, Moura I, LeGall J, Xavier AV, Sieker L. 1979. The amino acid sequence of desulforedoxin, a new type of non-heme iron protein from Desulfovibrio gigas. Biochem Biophys Res Commun 90:596-605.
    • (1979) Biochem Biophys Res Commun , vol.90 , pp. 596-605
    • Bruschi, M.1    Moura, I.2    LeGall, J.3    Xavier, A.V.4    Sieker, L.5
  • 10
    • 0027453522 scopus 로고
    • Cadmium-113 nuclear magnetic resonance applied to metalloproteins
    • Coleman JE. 1993. Cadmium-113 nuclear magnetic resonance applied to metalloproteins. Methods Enzymol 227:16-43.
    • (1993) Methods Enzymol , vol.227 , pp. 16-43
    • Coleman, J.E.1
  • 11
    • 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
  • 13
    • 0026089657 scopus 로고
    • Efficient computation of three-dimensional proteins structures in solution from NMR data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA
    • Güntert P, Braun W, Wüthrich K. 1991a. Efficient computation of three-dimensional proteins structures in solution from NMR data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA. J Mol Biol 217:517-530.
    • (1991) J Mol Biol , vol.217 , pp. 517-530
    • Güntert, P.1    Braun, W.2    Wüthrich, K.3
  • 14
    • 0026259488 scopus 로고
    • Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints
    • Güntert P, Wüthrich K. 1991. Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints. J Biomol NMR 1:447-456.
    • (1991) J Biomol NMR , vol.1 , pp. 447-456
    • Güntert, P.1    Wüthrich, K.2
  • 15
    • 0026011496 scopus 로고
    • Structure determination of the Antp(C39-S) homodomain from NMR data in solution using a novel strategy for the structure calculation with the programs DIANA, CALIBA, HABAS and GLOMSA
    • Güntert P, Yan QQ, Otting G, Müller M, Gehring W, Wüthrich K. 1991b. Structure determination of the Antp(C39-S) homodomain from NMR data in solution using a novel strategy for the structure calculation with the programs DIANA, CALIBA, HABAS and GLOMSA. J Mol Biol 217:531-540.
    • (1991) J Mol Biol , vol.217 , pp. 531-540
    • Güntert, P.1    Yan, Q.Q.2    Otting, G.3    Müller, M.4    Gehring, W.5    Wüthrich, K.6
  • 17
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi R, Biliter M, Wuthrich K. 1996. MOLMOL: A program for display and analysis of macromolecular structures. J Mol Graphics 14:51-55.
    • (1996) J Mol Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Biliter, M.2    Wuthrich, K.3
  • 18
    • 0017389657 scopus 로고
    • Isolation and characterization of desulforedoxin, a new type of non-heme 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 non-heme 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
  • 20
    • 0017844452 scopus 로고
    • A comparative spectroscopic study of two non-heme iron proteins lacking labile sulphide from Desulfovibrio gigas
    • Moura I, Xavier AV, Cammack R, Bruschi M, LeGall J. 1978. A comparative spectroscopic study of two non-heme iron proteins lacking labile sulphide from Desulfovibrio gigas. Biochim Biophys Acta 533:156-162.
    • (1978) Biochim Biophys Acta , vol.533 , pp. 156-162
    • Moura, I.1    Xavier, A.V.2    Cammack, R.3    Bruschi, M.4    LeGall, J.5
  • 21
    • 0031287732 scopus 로고    scopus 로고
    • Analysis, design and engineering of simple iron-sulfur proteins: Tales from rubredoxin and desulforedoxin
    • Moura JJG, Goodfellow BJ, Romão MJ, Rusnak F, Moura I. 1996. Analysis, design and engineering of simple iron-sulfur proteins: Tales from rubredoxin and desulforedoxin. Comments Inorg Chem 19:47-66.
    • (1996) Comments Inorg Chem , vol.19 , pp. 47-66
    • Moura, J.J.G.1    Goodfellow, B.J.2    Romão, M.J.3    Rusnak, F.4    Moura, I.5
  • 23
    • 0028673854 scopus 로고
    • Rubredoxin in crystalline state
    • Sieker LC. 1994. Rubredoxin in crystalline state. Methods Enzymol 243:47-66.
    • (1994) Methods Enzymol , vol.243 , pp. 47-66
    • Sieker, L.C.1
  • 24
    • 0002895832 scopus 로고
    • 113Cd spectroscopy of coordination compounds and proteins
    • 113Cd spectroscopy of coordination compounds and proteins. Coord Chem Rev 86:43-134.
    • (1988) Coord Chem Rev , vol.86 , pp. 43-134
    • Summers, M.F.1
  • 25
    • 0026597879 scopus 로고
    • The chemical shift index: A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy
    • Wishart DS, Sykes BD, Richards FM. 1992. The chemical shift index: A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry 31:1647-1651.
    • (1992) Biochemistry , vol.31 , pp. 1647-1651
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.