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Volumn 48, Issue 40, 2009, Pages 9525-9533

Plasmodium falciparum ferredoxin-NADP+ reductase His286 plays a dual role in NADP(H) binding and catalysis

Author keywords

[No Author keywords available]

Indexed keywords

ADENINE RING; ADENYLATE; AMP COMPLEX; CRYSTAL FORMS; DUAL ROLE; H-BONDING; PLASMODIUM FALCIPARUM; POSITIVELY CHARGED; SIDE CHAINS; SUBSTRATE RECOGNITION; SUBSTRATE-BINDING; TRANSFER RATES; WILD TYPES;

EID: 70350063832     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9013209     Document Type: Article
Times cited : (11)

References (27)
  • 3
    • 23844532238 scopus 로고    scopus 로고
    • + reductase/ferredoxin redox system as a possible drug target against apicomplexan human parasites
    • + reductase/ferredoxin redox system as a possible drug target against apicomplexan human parasites. Curr. Pharm. Des. 11, 3159-3172.
    • (2005) Curr. Pharm. Des. , vol.11 , pp. 3159-3172
    • Seeber, F.1    Aliverti, A.2    Zanetti, G.3
  • 5
    • 33845717210 scopus 로고    scopus 로고
    • The Expression of a Plant-type Ferredoxin Redox System provides Molecular Evidence for a Plastid in the Early Dinoflagellate Perkinsus marinus
    • DOI 10.1016/j.protis.2006.09.003, PII S1434461006001015
    • Stelter, K., El-Sayed, N. M., and Seeber, F. (2007) The expression of a plant-type ferredoxin redox system provides molecular evidence for a plastid in the early dinoflagellate Perkinsus marinus. Protist 158, 119-130. (Pubitemid 44969624)
    • (2007) Protist , vol.158 , Issue.1 , pp. 119-130
    • Stelter, K.1    El-Sayed, N.M.2    Seeber, F.3
  • 13
    • 0028921929 scopus 로고
    • Refined crystal structure of spinach ferredoxin reductase at 1.7 A° resolution: Oxidized, reduced and 2′-phospho-5′-AMP bound states
    • Bruns, C. M., and Karplus, P. A. (1995) Refined crystal structure of spinach ferredoxin reductase at 1.7 A° resolution: Oxidized, reduced and 2′-phospho-5′-AMP bound states. J. Mol. Biol. 247, 125-145.
    • (1995) J. Mol. Biol. , vol.247 , pp. 125-145
    • Bruns, C.M.1    Karplus, P.A.2
  • 16
    • 0026023225 scopus 로고
    • + reductase: Prototype for a structurally novel flavoenzyme family
    • + reductase: Prototype for a structurally novel flavoenzyme family. Science 251, 60-66.
    • (1991) Science , vol.251 , pp. 60-66
    • Karplus, P.A.1    Daniels, M.J.2    Herriott, J.R.3
  • 17
    • 0032612239 scopus 로고    scopus 로고
    • Identifying and quantitating FAD and FMN in simple and in iron-sulfur-containing flavoproteins
    • Aliverti, A., Curti, B., and Vanoni, M. A. (1999) Identifying and quantitating FAD and FMN in simple and in iron-sulfur-containing flavoproteins. Methods Mol. Biol. 131, 9-23.
    • (1999) Methods Mol. Biol. , vol.131 , pp. 9-23
    • Aliverti, A.1    Curti, B.2    Vanoni, M.A.3
  • 18
    • 0017716367 scopus 로고
    • A photochemical procedure for reduction of oxidation-reduction proteins employing deazariboflavin as catalyst
    • Massey, V., and Hemmerich, P. (1977) A photochemical procedure for reduction of oxidation-reduction proteins employing deazariboflavin as catalyst. J. Biol. Chem. 252, 5612-5614.
    • (1977) J. Biol. Chem. , vol.252 , pp. 5612-5614
    • Massey, V.1    Hemmerich, P.2
  • 19
    • 0033212815 scopus 로고    scopus 로고
    • Integration of macromolecular diffraction data
    • Leslie, A. G. W. (1999) Integration of macromolecular diffraction data. Acta Crystallogr. D55, 1696-1702.
    • (1999) Acta Crystallogr. , vol.55 , pp. 1696-1702
    • Leslie, A.G.W.1
  • 20
    • 0002584126 scopus 로고
    • Data reduction: Data correction and processing
    • Sawyer, L., Isaacs, N., and Bailey, S., Eds. Daresbury Laboratory, Warrington, U.K
    • Evans, P. R. (1993) Data reduction: Data correction and processing. In Proceedings of the CCP4 Study Weekend. Data Collection and Processing (Sawyer, L., Isaacs, N., and Bailey, S., Eds.) pp 114-123, Daresbury Laboratory, Warrington, U.K.
    • (1993) Proceedings of the CCP4 Study Weekend. Data Collection and Processing , pp. 114-123
    • Evans, P.R.1
  • 21
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An Automated Program for Molecular Replacement
    • Vagin, A., and Teplyakov, A. (1997) MOLREP: An Automated Program for Molecular Replacement. J. Appl. Crystallogr. 30, 1022-1025.
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 22
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of Macromolecular Structures by the Maximum-Likelihood Method
    • Murshudov, G. N., Vagin, A. A., and Dodson, E. J. (1997) Refinement of Macromolecular Structures by the Maximum-Likelihood Method. Acta Crystallogr. D53, 240-255.
    • (1997) Acta Crystallogr. , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.