1kll
From Proteopedia
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|PDB= 1kll |SIZE=350|CAPTION= <scene name='initialview01'>1kll</scene>, resolution 1.50Å | |PDB= 1kll |SIZE=350|CAPTION= <scene name='initialview01'>1kll</scene>, resolution 1.50Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=MC:1,2-CIS-1-HYDROXY-2,7-DIAMINO-MITOSENE'>MC</scene> | + | |LIGAND= <scene name='pdbligand=MC:1,2-CIS-1-HYDROXY-2,7-DIAMINO-MITOSENE'>MC</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1kmz|1KMZ]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kll FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kll OCA], [http://www.ebi.ac.uk/pdbsum/1kll PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kll RCSB]</span> | ||
}} | }} | ||
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[[Category: Sheffield, P.]] | [[Category: Sheffield, P.]] | ||
[[Category: Sherman, D.]] | [[Category: Sherman, D.]] | ||
| - | [[Category: MC]] | ||
[[Category: anomalous diffraction]] | [[Category: anomalous diffraction]] | ||
[[Category: antibiotic resistance]] | [[Category: antibiotic resistance]] | ||
| Line 41: | Line 43: | ||
[[Category: sad]] | [[Category: sad]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:50:14 2008'' |
Revision as of 18:50, 30 March 2008
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| , resolution 1.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Related: | 1KMZ
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Mar 30 21:50:14 2008
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. | Anomalous diffraction | Antibiotic resistance | Crystal structure | Domain swapping | Mitomycin c | P-staking | Sad
