메뉴 건너뛰기




Volumn 11, Issue 9, 2002, Pages 2125-2137

A structurally conserved water molecule in Rossmann dinucleotide-binding domains

Author keywords

Dinucleotide protein interactions; FAD; Molecular recognition; NAD; NADP; Rossmann fold; Structurally conserved water molecule

Indexed keywords

APOENZYME; DINUCLEOTIDE; ENZYME; FLAVINE ADENINE NUCLEOTIDE; GLYCINE; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; PHOSPHATE; PYROPHOSPHATE; SOLVENT; WATER; BACTERIAL PROTEIN; FUNGAL PROTEIN; PROTOZOAL PROTEIN; VEGETABLE PROTEIN;

EID: 0036707995     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.0213502     Document Type: Article
Times cited : (136)

References (120)
  • 9
    • 0035896010 scopus 로고    scopus 로고
    • Crystal structure of the catalytic core component of the alkylhydroperoxide reductase AhpF from Escherichia coli
    • (2001) J. Mol. Biol. , vol.307 , pp. 1-8
    • Bieger, B.1    Essen, L.O.2
  • 20
    • 0030893657 scopus 로고    scopus 로고
    • NADP-dependent enzymes. I: Conserved stereochemistry of cofactor binding
    • (1997) Proteins , vol.28 , pp. 10-28
    • Carugo, O.1    Argos, P.2
  • 36
    • 0027302991 scopus 로고
    • Crystal structure of a ternary complex of Escherichia coli malate dehydrogenase citrate and NAD at 1.9 Å resolution
    • (1993) J. Mol. Biol. , vol.232 , pp. 213-222
    • Hall, M.D.1    Banaszak, L.J.2
  • 37
    • 0035811098 scopus 로고    scopus 로고
    • Probing catalysis by Escherichia coli dTDP-glucose-4,6-dehydratase: Identification and preliminary characterization of functional amino acid residues at the active site
    • (2001) Biochemistry , vol.40 , pp. 6598-6610
    • Hegeman, A.D.1    Gross, J.W.2    Frey, P.A.3
  • 39
    • 0033572790 scopus 로고    scopus 로고
    • Wet and dry interfaces: The role of solvent in protein-protein and protein-DNA recognition
    • (1999) Struct. Fold. Des. , vol.7
    • Janin, J.1
  • 43
    • 0024421234 scopus 로고
    • Substrate binding and catalysis by glutathione reductase as derived from refined enzyme: Substrate crystal structures at 2 Å resolution
    • (1989) J. Mol. Biol. , vol.210 , pp. 163-180
  • 51
  • 62
    • 0028333861 scopus 로고
    • Structure of glutathione reductase from Escherichia coil at 1.86 Å resolution: Comparison with the enzyme from human erythrocytes
    • (1994) Protein Sci. , vol.3 , pp. 799-809
    • Mittl, P.R.1    Schulz, G.E.2
  • 80
    • 0031015737 scopus 로고    scopus 로고
    • Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: Crystallographic evidence
    • (1997) Biochemistry , vol.36 , pp. 586-603
    • Sawaya, M.R.1    Kraut, J.2
  • 94
    • 0029849211 scopus 로고    scopus 로고
    • High-resolution X-ray structure of UDP-galactose 4-epimerase complexed with UDP-phenol
    • (1996) Protein Sci. , vol.5 , pp. 2149-2161
  • 95
    • 0029921058 scopus 로고    scopus 로고
    • Molecular structure of the NADH/UDP-glucose abortive complex of UDP-galactose 4-epimerase from Escherichia coli: Implications for the catalytic mechanism
    • (1996) Biochemistry , vol.35 , pp. 5137-5144
  • 98
    • 0035805630 scopus 로고    scopus 로고
    • Human UDP-galactose 4-epimerase. Accomodation of UDP-N-acetylglcosamine within the active site
    • (2001) J. Biol. Chem. , vol.276 , pp. 15131-15136


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.