The crystal structure of glutathione

Abstract

The tripeptide glutathione (y-~.-glutamyl-~-cysteinyl-glycine, Cx0H~;NaO~S) crystallizes in the orthorhombie system with space group P2~2~2~ and unit-cell dimensions a = 28-054-0-02, b----8.802+0"002, c = 5"630___0.002 A. The positions of the sulphur atoms in the unit cell were determined from the Harker sections of the three-dimensional Patterson ftmction.The structure was finally determined from a c-axis Fourier projection pattern based on terms with signs derived by the method of Cochran & Douglas, used in conjunction with a three-dimensional electron-density distribution based on terms with phase angles given by the sulphur atoms only. The structure was refined by two-and three-dimensional Fourier s:~ntheses.The molecule contains no unusual bond lengths or angles and adopts a curled configuration with the planes of the glycine carboxyl group and the amino-carboxyl group both parallel to the c-axis, and the planar peptide linkages inclined at 94-4 ° to one another. The sulphur atoms form zigzag chains about alternate screw diad axes parallel to c, the S-S distance being 4.41 A. The structure is held together by a three-dimensional network of hydrogen bonds, but there are no internal hydrogen bonds in the molecule.

N-t-Butyloxycarbonyl-S-benzylcysteinylglycine methyl ester

“…H(8) The C-S bond lengths and the C-S-C bond angle H(9) are in agreement with the corresponding values found H(10) H(ll) in glutathione (1.78A, Wright, 1958) .…”

Structure of human χχ alcohol dehydrogenase: a glutathione-dependent formaldehyde dehydrogenase

“…As a first step for these modeling studies, we surveyed the three-dimensional structures of GSH. In the crystalline state, GSH exhibits an extended Y-shape conformation (Wright, 1958), which is similar to the low-energy conformation Cedergren-Zeppezauer et al (1985 suggested that there are intermediate conformational states between the fully open and the fully closed conformations in ADH. This suggestion was based on a ''partially closed'' conformation observed in the Cys46-carboxymethylated EE-NADH structure.…”

Conformation and structure of α-L-glutamyl-L-glutamic acid

“…We felt that such a study was of particular value since, at the outset of our program, no crystallographic information on any linear peptide containing either Asp or Gla was available, and the only structural studies of Glu peptides involved the fully blocked dipeptide Z-(y-ethyl)-L-Glu-(Fethyl)-L-Glu-ethyl ester (Benedetti, DiBlasio, Pavone, Pedone, Germain & Goodman, 1979) and the y-glutamyl tripeptide glutathione (Wright, 1958). We have recently provided accounts of the crystal and molecular structures of the (Valente, Hiskey & Hodgson, 1979), and the free dipeptides tx-L-Asp-Gly.H20 (Eggleston, Valente & Hodgson, 1981a), ct-L-Glu-Gly (Eggleston, Valente & Hodgson, 1981b), and Gly-L-Asp.2H20 (Eggleston & Hodgson, 1981).…”