1kll

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(New page: 200px<br /><applet load="1kll" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kll, resolution 1.50&Aring;" /> '''MOLECULAR BASIS OF M...)
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caption="1kll, resolution 1.50&Aring;" />
'''MOLECULAR BASIS OF MITOMYCIN C RESICTANCE IN STREPTOMYCES: CRYSTAL STRUCTURES OF THE MRD PROTEIN WITH AND WITHOUT A DRUG DERIVATIVE'''<br />
'''MOLECULAR BASIS OF MITOMYCIN C RESICTANCE IN STREPTOMYCES: CRYSTAL STRUCTURES OF THE MRD PROTEIN WITH AND WITHOUT A DRUG DERIVATIVE'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1KLL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_lavendulae Streptomyces lavendulae] with MC as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KLL OCA].
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1KLL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_lavendulae Streptomyces lavendulae] with <scene name='pdbligand=MC:'>MC</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KLL OCA].
==Reference==
==Reference==
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[[Category: Dauter, Z.]]
[[Category: Dauter, Z.]]
[[Category: Derewenda, U.]]
[[Category: Derewenda, U.]]
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[[Category: Derewenda, Z.S.]]
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[[Category: Derewenda, Z S.]]
[[Category: Devedjiev, Y.]]
[[Category: Devedjiev, Y.]]
[[Category: He, M.]]
[[Category: He, M.]]
[[Category: Jelen, F.]]
[[Category: Jelen, F.]]
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[[Category: Martin, T.W.]]
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[[Category: Martin, T W.]]
[[Category: Otlewski, J.]]
[[Category: Otlewski, J.]]
[[Category: Sheffield, P.]]
[[Category: Sheffield, P.]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 01:33:29 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:35:26 2008''

Revision as of 11:35, 21 February 2008

Image:1kll.jpg

1kll, resolution 1.50Å

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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 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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