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Volumn 7, Issue , 2007, Pages

Crystal structures of Leptospira interrogans FAD-containing ferredoxin-NADP+ reductase and its complex with NADP+

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; FERREDOXIN NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE REDUCTASE; FLAVINE ADENINE NUCLEOTIDE; FLAVOPROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; ASPARTIC ACID;

EID: 37349085779     PISSN: None     EISSN: 14726807     Source Type: Journal    
DOI: 10.1186/1472-6807-7-69     Document Type: Article
Times cited : (19)

References (39)
  • 1
    • 2342565785 scopus 로고    scopus 로고
    • Functional plasticity and catalytic efficiency in plant and bacterial ferredoxin-NADP(H) reductases
    • Functional plasticity and catalytic efficiency in plant and bacterial ferredoxin-NADP(H) reductases. EA Ceccarelli AK Arakaki N Cortez N Carrillo, Biochim Biophys Acta 2004 1968 155 165
    • (2004) Biochim Biophys Acta , vol.1968 , pp. 155-165
    • Ceccarelli, E.A.1    Arakaki, A.K.2    Cortez, N.3    Carrillo, N.4
  • 2
    • 33751237715 scopus 로고    scopus 로고
    • Reduction of the pea ferredoxin-NADP(H) reductase catalytic efficiency by the structuring of a carboxyl-terminal artificial metal binding site
    • 10.1021/bi061152v. 17105208
    • Reduction of the pea ferredoxin-NADP(H) reductase catalytic efficiency by the structuring of a carboxyl-terminal artificial metal binding site. DL Catalano-Dupuy M Orecchia DV Rial EA Ceccarelli, Biochemistry 2006 45 13899 13909 10.1021/bi061152v 17105208
    • (2006) Biochemistry , vol.45 , pp. 13899-13909
    • Catalano-Dupuy, D.L.1    Orecchia, M.2    Rial, D.V.3    Ceccarelli, E.A.4
  • 4
    • 0028921929 scopus 로고
    • Refined crystal structure of spinach ferredoxin reductase at 1.7 a resolution: Oxidized, reduced and 2'-phospho-5'-AMP bound states
    • 10.1006/jmbi.1994.0127. 7897656
    • Refined crystal structure of spinach ferredoxin reductase at 1.7 A resolution: oxidized, reduced and 2'-phospho-5'-AMP bound states. CM Bruns PA Karplus, J Mol Biol 1995 247 125 145 10.1006/jmbi.1994.0127 7897656
    • (1995) J Mol Biol , vol.247 , pp. 125-145
    • Bruns, C.M.1    Karplus, P.A.2
  • 8
    • 0031585989 scopus 로고    scopus 로고
    • The three dimensional structure of flavodoxin reductase from Escherichia coli at 1.7 a resolution
    • 10.1006/jmbi.1997.0957. 9149148
    • The three dimensional structure of flavodoxin reductase from Escherichia coli at 1.7 A resolution. M Ingelman V Bianchi H Eklund, J Mol Biol 1997 268 147 157 10.1006/jmbi.1997.0957 9149148
    • (1997) J Mol Biol , vol.268 , pp. 147-157
    • Ingelman, M.1    Bianchi, V.2    Eklund, H.3
  • 10
    • 4043167104 scopus 로고    scopus 로고
    • Structural aspects of Plants Ferredoxin:NADP(+) Oxidoreductases
    • 10.1023/B:PRES.0000036884.57303.2e. 16034534
    • Structural aspects of Plants Ferredoxin:NADP(+) Oxidoreductases. PA Karplus HR Faber, Photosynthesis Research 2004 81 303 315 10.1023/B:PRES. 0000036884.57303.2e 16034534
    • (2004) Photosynthesis Research , vol.81 , pp. 303-315
    • Karplus, P.A.1    Faber, H.R.2
  • 11
    • 0038368151 scopus 로고    scopus 로고
    • + reductase catalytic mechanism
    • 10.1046/j.1432-1033.2003.03566.x. 12709048
    • + reductase catalytic mechanism. N Carrillo EA Ceccarelli, Eur J Biochem 2003 270 1900 1915 10.1046/j.1432-1033.2003.03566.x 12709048
    • (2003) Eur J Biochem , vol.270 , pp. 1900-1915
    • Carrillo, N.1    Ceccarelli, E.A.2
  • 13
    • 33847093343 scopus 로고    scopus 로고
    • +-dependent Dimerization and Inactivation: Functional and Crystallographic Analysis
    • 10.1016/j.jmb.2007.01.005. 17258767
    • +-dependent Dimerization and Inactivation: Functional and Crystallographic Analysis. M Milani E Balconi A Aliverti E Mastrangelo F Seeber M Bolognesi G Zanetti, J Mol Biol 2007 367 501 513 10.1016/j.jmb.2007.01. 005 17258767
    • (2007) J Mol Biol , vol.367 , pp. 501-513
    • Milani, M.1    Balconi, E.2    Aliverti, A.3    Mastrangelo, E.4    Seeber, F.5    Bolognesi, M.6    Zanetti, G.7
  • 16
    • 0021770735 scopus 로고
    • + and ferrodoxin
    • 6746626
    • + and ferrodoxin. CJ Batie H Kamin, J Biol Chem 1984 259 8832 8839 6746626
    • (1984) J Biol Chem , vol.259 , pp. 8832-8839
    • Batie, C.J.1    Kamin, H.2
  • 17
    • 33745727134 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction studies of ferredoxin reductase from Leptospira interrogans
    • Crystallization and preliminary X-ray diffraction studies of ferredoxin reductase from Leptospira interrogans. AS Nascimento T Ferrarezi DL Catalano-Dupuy EA Ceccarelli I Polikarpov, Acta Cryst 2006 F62 662 664
    • (2006) Acta Cryst , vol.62 , pp. 662-664
    • Nascimento, A.S.1    Ferrarezi, T.2    Catalano-Dupuy, D.L.3    Ceccarelli, E.A.4    Polikarpov, I.5
  • 19
    • 0032365636 scopus 로고    scopus 로고
    • Set-up and experimental parameters of the protein crystallography beamline at the brazilian national synchrotron laboratory
    • 10.1107/S0909049597014684
    • Set-up and experimental parameters of the protein crystallography beamline at the brazilian national synchrotron laboratory. I Polikarpov LA Perles RT de Oliveira G Oliva EE Castellano RC Garratt A Craievich, J Synchrotron Rad 1998 5 72 76 10.1107/S0909049597014684
    • (1998) J Synchrotron Rad , vol.5 , pp. 72-76
    • Polikarpov, I.1    Perles, L.A.2    De Oliveira, R.T.3    Oliva, G.4    Castellano, E.E.5    Garratt, R.C.6    Craievich, A.7
  • 20
    • 0030781401 scopus 로고    scopus 로고
    • The ultimate wavelength for protein crystallography?
    • The ultimate wavelength for protein crystallography? I Polikarpov A Teplyakov G Oliva, Acta Cryst 1997 D53 734 737
    • (1997) Acta Cryst , vol.53 , pp. 734-737
    • Polikarpov, I.1    Teplyakov, A.2    Oliva, G.3
  • 21
    • 0032128261 scopus 로고    scopus 로고
    • On the choice of an optimal wavelength in macromolecular crystallography
    • On the choice of an optimal wavelength in macromolecular crystallography. A Teplyakov G Oliva I Polikarpov, Acta Cryst 1998 D54 610 614
    • (1998) Acta Cryst , vol.54 , pp. 610-614
    • Teplyakov, A.1    Oliva, G.2    Polikarpov, I.3
  • 22
    • 0003076963 scopus 로고
    • Recent changes to the MOSFLM package for processing film and image plate data
    • Recent changes to the MOSFLM package for processing film and image plate data. AGW Leslie, Jnt CCP4/ESF-EACBM Newsl Protein Crystallogr 1992 26
    • (1992) Jnt CCP4/ESF-EACBM Newsl Protein Crystallogr , pp. 26
    • Leslie, A.G.W.1
  • 23
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • COLLABORATIVE COMPUTATIONAL PROJECT, NUMBER 4
    • The CCP4 suite: programs for protein crystallography. COLLABORATIVE COMPUTATIONAL PROJECT, NUMBER 4, Acta Cryst 1994 D50 760 763
    • (1994) Acta Cryst , vol.50 , pp. 760-763
  • 24
    • 0035807852 scopus 로고    scopus 로고
    • Biochemical and crystallographic characterization of ferrodoxin-NADP(+) reductase from nonphotosynthetic tissues
    • 10.1021/bi011224c. 11724563
    • Biochemical and crystallographic characterization of ferrodoxin-NADP(+) reductase from nonphotosynthetic tissues. A Aliverti R Faber CM Finnerty C Ferioli V Pandini A Negri PA Karplus G Zanetti, Biochemistry 2001 40 14501 14508 10.1021/bi011224c 11724563
    • (2001) Biochemistry , vol.40 , pp. 14501-14508
    • Aliverti, A.1    Faber, R.2    Finnerty, C.M.3    Ferioli, C.4    Pandini, V.5    Negri, A.6    Karplus, P.A.7    Zanetti, G.8
  • 27
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Coot: model-building tools for molecular graphics. P Emsley K Cowtan, Acta Cryst 2004 D60 2126 2132
    • (2004) Acta Cryst , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 29
    • 0036816606 scopus 로고    scopus 로고
    • Advances in structure analysis using small-angle scattering in solution
    • 10.1016/S0959-440X(02)00363-9. 12464319
    • Advances in structure analysis using small-angle scattering in solution. DI Svergun MHJ Koch, Curr Opin Struct Biol 2002 12 5 654 60 10.1016/S0959- 440X(02)00363-9 12464319
    • (2002) Curr Opin Struct Biol , vol.12 , Issue.5 , pp. 654-60
    • Svergun, D.I.1    Koch, M.H.J.2
  • 31
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using peeceptual criteria
    • 10.1107/S0021889892001663
    • Determination of the regularization parameter in indirect-transform methods using peeceptual criteria. DI Svergun, J Appl Crystallogr 1992 25 495 503 10.1107/S0021889892001663
    • (1992) J Appl Crystallogr , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 32
    • 0035010533 scopus 로고    scopus 로고
    • Determination of domain structure of proteins from X-ray solution scattering
    • 11371467
    • Determination of domain structure of proteins from X-ray solution scattering. DI Svergun MV Petoukhov MHJ Koch, Biophys J 2001 80 2946 2953 11371467
    • (2001) Biophys J , vol.80 , pp. 2946-2953
    • Svergun, D.I.1    Petoukhov, M.V.2    Koch, M.H.J.3
  • 33
    • 0035124442 scopus 로고    scopus 로고
    • Automated matching of high- and low-resolution structural models
    • 10.1107/S0021889800014126
    • Automated matching of high- and low-resolution structural models. MB Kozin DI Svergun, J Appl Crystallog 2001 34 33 41 10.1107/S0021889800014126
    • (2001) J Appl Crystallog , vol.34 , pp. 33-41
    • Kozin, M.B.1    Svergun, D.I.2
  • 34
    • 0029185933 scopus 로고
    • CRYSOL - A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • 10.1107/S0021889895007047
    • CRYSOL - a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates. DI Svergun C Barberato MH Koch, Appl Crystallogr 1995 28 768 773 10.1107/S0021889895007047
    • (1995) Appl Crystallogr , vol.28 , pp. 768-773
    • Svergun, D.I.1    Barberato, C.2    Koch, M.H.3
  • 35
    • 0017187522 scopus 로고
    • A lysyl residue at the NADP binding site of ferredoxin-NADP reductase
    • 8135
    • A lysyl residue at the NADP binding site of ferredoxin-NADP reductase. G Zanetti, Biochim Biophys Acta 1976 445 14 24 8135
    • (1976) Biochim Biophys Acta , vol.445 , pp. 14-24
    • Zanetti, G.1
  • 36
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: Multiple sequence alignment with high accuracy and high throughput
    • 15034147. 10.1093/nar/gkh340
    • MUSCLE: multiple sequence alignment with high accuracy and high throughput. RC Edgar, Nucleic Acids Research 2004 32 1792 1797 15034147 10.1093/nar/gkh340
    • (2004) Nucleic Acids Research , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 37
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: Analysis of multiple sequence alignments in PostScript
    • 10.1093/bioinformatics/15.4.305. 10320398
    • ESPript: analysis of multiple sequence alignments in PostScript. P Gouet E Courcelle DI Stuart F Metoz, Bioinformatics 1999 15 305 308 10.1093/bioinformatics/15.4.305 10320398
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4
  • 39
    • 0028922586 scopus 로고
    • LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions
    • 10.1093/protein/8.2.127
    • LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. AC Wallace RA Laskowski JM Thornton, Prot Eng 1995 8 127 134 10.1093/protein/8.2.127
    • (1995) Prot Eng , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3


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