PMID:8635474: Difference between revisions
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!align=left |Citation | |||
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'''Lewis, RJ, Singh, OM, Smith, CV, Skarzynski, T, Maxwell, A, Wonacott, AJ and Wigley, DB''' (1996) The nature of inhibition of DNA gyrase by the coumarins and the cyclothialidines revealed by X-ray crystallography. ''EMBO J.'' '''15''':1412-20 | |||
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!align=left |Abstract | |||
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This study describes the first crystal structures of a complex between a DNA topoisomerase and a drug. We present the structures of a 24 kDa N-terminal fragment of the Escherichia coli DNA gyrase B protein in complexes with two different inhibitors of the ATPase activity of DNA gyrase, namely the coumarin antibiotic, novobiocin, and GR122222X, a member of the cyclothialidine family. These structures are compared with the crystal structure of the complex with an ATP analogue, adenylyl-beta-gamma-imidodiphosphate (ADPNP). The likely mechanism, by which mutant gyrase B proteins become resistant to inhibition by novobiocin are discussed in light of these comparisons. The three ligands are quite dissimilar in chemical structure and bind to the protein in very different ways, but their binding is competitive because of a small degree of overlap of their binding sites. These crystal structures consequently describe a chemically well characterized ligand binding surface and provide useful information to assist in the design of novel ligands. | |||
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8635474 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC450046 PMC450046] | |||
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!align=left |Keywords | |||
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Adenylyl Imidodiphosphate/chemistry; Crystallography, X-Ray; DNA Gyrase; DNA Topoisomerases, Type II/chemistry; Enzyme Inhibitors/chemistry; Escherichia coli/chemistry; Escherichia coli/enzymology; Models, Molecular; Novobiocin/chemistry; Peptide Fragments/chemistry; Peptides, Cyclic/chemistry; Topoisomerase II Inhibitors | |||
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==Significance {{HelpIcon|Help:Literature}} == | |||
{{LitSignificance}} | |||
== Useful Materials and Methods {{HelpIcon|Help:Literature}}== | |||
{{LitMaterials}} | |||
==Annotations {{HelpIcon|Help:Literature}}== | |||
<annotationlinks/> | |||
==EcoliWiki Links {{HelpIcon|Help:Literature}} == | |||
{{LitLinks}} | |||
==See also== | |||
==References== | |||
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Latest revision as of 04:26, 16 July 2014
| Citation |
Lewis, RJ, Singh, OM, Smith, CV, Skarzynski, T, Maxwell, A, Wonacott, AJ and Wigley, DB (1996) The nature of inhibition of DNA gyrase by the coumarins and the cyclothialidines revealed by X-ray crystallography. EMBO J. 15:1412-20 |
|---|---|
| Abstract |
This study describes the first crystal structures of a complex between a DNA topoisomerase and a drug. We present the structures of a 24 kDa N-terminal fragment of the Escherichia coli DNA gyrase B protein in complexes with two different inhibitors of the ATPase activity of DNA gyrase, namely the coumarin antibiotic, novobiocin, and GR122222X, a member of the cyclothialidine family. These structures are compared with the crystal structure of the complex with an ATP analogue, adenylyl-beta-gamma-imidodiphosphate (ADPNP). The likely mechanism, by which mutant gyrase B proteins become resistant to inhibition by novobiocin are discussed in light of these comparisons. The three ligands are quite dissimilar in chemical structure and bind to the protein in very different ways, but their binding is competitive because of a small degree of overlap of their binding sites. These crystal structures consequently describe a chemically well characterized ligand binding surface and provide useful information to assist in the design of novel ligands. |
| Links | |
| Keywords |
Adenylyl Imidodiphosphate/chemistry; Crystallography, X-Ray; DNA Gyrase; DNA Topoisomerases, Type II/chemistry; Enzyme Inhibitors/chemistry; Escherichia coli/chemistry; Escherichia coli/enzymology; Models, Molecular; Novobiocin/chemistry; Peptide Fragments/chemistry; Peptides, Cyclic/chemistry; Topoisomerase II Inhibitors |
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