1kll

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spinqualitylabelsall models 1kll, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

MOLECULAR BASIS OF MITOMYCIN C RESICTANCE IN STREPTOMYCES: CRYSTAL STRUCTURES OF THE MRD PROTEIN WITH AND WITHOUT A DRUG DERIVATIVE

Overview

Mitomycin C (MC) is a potent anticancer agent. Streptomyces lavendulae, which produces MC, protects itself from the lethal effects of the drug by, expressing several resistance proteins. One of them (MRD) binds MC and, functions as a drug exporter. We report the crystal structure of MRD and, its complex with an MC metabolite, 1,2-cis-1-hydroxy-2,7-diaminomitosene, at 1.5 A resolution. The drug is sandwiched by pi-stacking interactions of, His-38 and Trp-108. MRD is a dimer. The betaalphabetabetabeta fold of the, MRD molecule is reminiscent of methylmalonyl-CoA epimerase, bleomycin, resistance proteins, glyoxalase I, and extradiol dioxygenases. The, location of the binding site is identical to the ones in evolutionarily, related enzymes, suggesting that the protein may have been recruited from, a different metabolic pathway.

About this Structure

1KLL is a Single protein structure of sequence from Streptomyces lavendulae with MC as ligand. Full crystallographic information is available from OCA.

Reference

Molecular basis of mitomycin C resistance in streptomyces: structure and function of the MRD protein., Martin TW, Dauter Z, Devedjiev Y, Sheffield P, Jelen F, He M, Sherman DH, Otlewski J, Derewenda ZS, Derewenda U, Structure. 2002 Jul;10(7):933-42. PMID:12121648

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