1kll
From Proteopedia
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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
Page seeded by OCA on Sun Nov 25 01:33:29 2007
Categories: Single protein | Streptomyces lavendulae | Dauter, Z. | Derewenda, U. | Derewenda, Z.S. | Devedjiev, Y. | He, M. | Jelen, F. | Martin, T.W. | Otlewski, J. | Sheffield, P. | Sherman, D. | MC | Anomalous diffraction | Antibiotic resistance | Crystal structure | Domain swapping | Mitomycin c | P-staking | Sad
