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Substrate binding and catalysis by glutathione reductase as derived from refined enzyme: substrate crystal structures at 2 A resolution.

Karplus PA, Schulz GE
J Mol Biol 210 163-80 (1989)
Related entries: 1grb, 1gre, 1grf, 1grg

Cited: 144 times
EuropePMC logo PMID: 2585516

Abstract

The X-ray structure analyses of four glutathione reductase complexes and derivatives have been extended to 2 A resolution and refined. The results are discussed in conjunction with the structure of the oxidized native enzyme known at 1.54 A resolution. While the residual co-ordinate errors are around 0.2 A, some significant shifts even in this range could be established. Points of particular interest are the 3.2 A approach of C4N of nicotinamide to N5F of flavin in hydride transfer geometry, the hydrogen bond geometries of the 2'-phosphate of NADPH as compared to inferior geometries for an inorganic phosphate binding together with NADH, the differential mobilities of parts of the substrates as derived from refined atomic temperature factors, and the stabilization of the thiolate of the proximal Cys63 by conformational changes of neighboring residues as well as by flavin. In addition, catalytically competent His467' is seen to interact more optimally with the sulfur of glutathione-I than with the distal sulfur of Cys58. The observed participation of water molecules for both NADPH and glutathione binding is so extensive that a prediction of the binding mode merely from the polypeptide structure would be very difficult. The accurately known geometries allowed us to draw some conclusions on the enzyme mechanism and suggest a possible scenario of the catalysis.

Reviews - 1gra mentioned but not cited (1)

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  1. Inhibition of Human Glutathione Reductase by the Nitrosourea Drugs 1,3-Bis(2-Chloroethyl)-1-Nitrosourea and 1-(2-Chloroethyl)-3-(2-Hydroxyethyl)-1-Nitrosourea. Karplus PA, Krauth-Siegel RL, Schirmer RH, Schulz GE Eur. J. Biochem. 171 193- (1988)
  2. Refined Structure of Glutathione Reductase at 1.54 Angstroms Resolution. Karplus PA, Schulz GE J. Mol. Biol. 195 701- (1987)
  3. Interaction of a glutathione S-conjugate with glutathione reductase. Kinetic and X-ray crystallographic studies.. Bilzer M, Krauth-Siegel RL, Schirmer RH, Akerboom TP, Sies H, Schulz GE Eur J Biochem 138 373-8 (1984)
  4. Comparison of the three-dimensional protein and nucleotide structure of the FAD-binding domain of p-hydroxybenzoate hydroxylase with the FAD- as well as NADPH-binding domains of glutathione reductase.. Wierenga RK, Drenth J, Schulz GE J Mol Biol 167 725-39 (1983)
  5. The catalytic mechanism of glutathione reductase as derived from x-ray diffraction analyses of reaction intermediates.. Pai EF, Schulz GE J Biol Chem 258 1752-7 (1983)
  6. Fad-Binding Site of Glutathione Reductase. Schulz GE, Schirmer RH, Pai EF J. Mol. Biol. 160 287- (1982)
  7. Glutathione reductase from human erythrocytes. The sequences of the NADPH domain and of the interface domain.. Krauth-Siegel RL, Blatterspiel R, Saleh M, Schiltz E, Schirmer RH, Untucht-Grau R Eur J Biochem 121 259-67 (1982)
  8. Three-Dimensional Structure of Glutathione Reductase at 2 Angstroms Resolution. Thieme R, Pai EF, Schirmer RH, Schulz GE J. Mol. Biol. 152 763- (1981)
  9. Gene Duplication in Glutathione Reductase. Schulz GE J. Mol. Biol. 138 335- (1980)
  10. The C-terminal fragment of human glutathione reductase contains the postulated catalytic histidine.. Untucht-Grau R, Schulz GE, Schirmer RH FEBS Lett 105 244-8 (1979)
  11. The structure of the flavoenzyme glutathione reductase.. Schulz GE, Schirmer RH, Sachsenheimer W, Pai EF Nature 273 120-4 (1978)
  12. Low resolution structure of human erythrocyte glutathione reductase.. Zappe HA, Krohne-Ehrich G, Schulz GE J Mol Biol 113 141-52 (1977)
  13. Crystals of Human Erythrocyte Glutathione Reductase. Schulz GE, Zappe H, Worthington DJ, Rosemeyer MA FEBS Lett. 54 86- (1975)

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