1ml6

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spinqualitylabelsall models PDB ID 1ml6 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
, resolution 1.90Å
Ligands:	and
Gene:	GST (Mus musculus)
Activity:	Glutathione transferase, with EC number 2.5.1.18
Coordinates:	save as pdb, mmCIF, xml

Crystal Structure of mGSTA2-2 in Complex with the Glutathione Conjugate of Benzo[a]pyrene-7(R),8(S)-Diol-9(S),10(R)-Epoxide

Overview

Murine class alpha glutathione S-transferase subunit types A2 (mGSTA2-2) and A1 (mGSTA1-1) have high catalytic efficiency for glutathione (GSH) conjugation of the ultimate carcinogenic metabolite of benzo[a]pyrene, (+)-anti-7,8-dihydroxy-9,10-oxy-7,8,9,10-tetrahydrobenzo[a]pyrene, [(+)-anti-BPDE]. Only 10 residues differ between the sequences of mGSTA1-1 and 2-2. However, the catalytic efficiency of mGSTA1-1 for GSH conjugation of (+)-anti-BPDE is >3-fold higher as compared with mGSTA2-2. The crystal structure of mGSTA1-1 in complex with the GSH conjugate of (+)-anti-7,8-dihydroxy-9,10-oxy-7,8,9,10-tetrahydrobenzo[a]pyrene (GSBpd) reveals that R216 and I221 in the last helix play important roles in catalysis [Gu, Y., Singh, S. V., and Ji, X. (2000) Biochemistry 39, 12552-12557]. The crystal structure of mGSTA2-2 in complex with GSBpd has been determined, which reveals a different binding mode of GSBpd. Comparison of the two structures suggests that residues 207 and 221 are responsible for the different binding mode of GSBpd and therefore contribute to the distinct catalytic efficiency of the two isozymes.

About this Structure

1ML6 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

Residues 207, 216, and 221 and the catalytic activity of mGSTA1-1 and mGSTA2-2 toward benzo[a]pyrene-(7R,8S)-diol-(9S,10R)-epoxide., Gu Y, Xiao B, Wargo HL, Bucher MH, Singh SV, Ji X, Biochemistry. 2003 Feb 4;42(4):917-21. PMID:12549910

Page seeded by OCA on Thu Mar 20 12:44:49 2008