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X-ray crystal structures of cytosolic glutathione S-transferases

Implications for protein architecture, substrate recognition and catalytic function

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EJB Reviews 1994

Part of the book series: EJB Reviews 1994 ((EJB REVIEWS,volume 1994))

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Abstract

Crystal structures of cytosolic glutathione S-transferases (EC 2.5.1.18), complexed with glutathione or its analogues, are reviewed. The atomic models define protein architectural relationships between the different gene classes in the superfamily, and reveal the molecular basis for substrate binding at the two adjacent subsites of the active site. Considerable progress has been made in understanding the mechanism whereby the thiol group of glutathione is destabilized (lowering its pK a) at the active site, a rate-enhancement strategy shared by the soluble glutathione S-trans- ferases.

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Abbreviations

GST:

glutathione S-transferase

pGSTP1-1, hGSTA1-1, rGSTM1-1 etc.:

acronyms for the glutathione S-transferases (GST)

p:

porcine

h:

human

r:

rat

b:

bovine

m:

mouse

rb:

rabbit

c:

chicken

gp:

guinea pig

P:

gene class pi

A:

gene class alpha

M:

gene class mu respectively

1-1:

indicates a dimer of two type-1 subunits

GSH:

reduced glutathione

P1, P2 etc. and G1, G2 etc.:

designate peptide functional groups in glutathione and the corresponding G-site ligands of the glutathione 5-transferases, respectively

G-site:

glutathione-binding site

H-site:

hydrophobic electrophile-binding site.

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  1. Department of Biochemistry, University of the Witwatersrand, PO Wits, Johannesburg, 2050, South Africa

    Heini Dirr

  2. Max-Planck-Institut für Biochemie, Martinsried, Germany

    Heini Dirr, Peter Reinemer & Robert Huber

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Dirr, H., Reinemer, P., Huber, R. (1994). X-ray crystal structures of cytosolic glutathione S-transferases. In: EJB Reviews 1994. EJB Reviews 1994, vol 1994. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-79502-2_5

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