1kzn
From Proteopedia
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'''Crystal Structure of E. coli 24kDa Domain in Complex with Clorobiocin''' | '''Crystal Structure of E. coli 24kDa Domain in Complex with Clorobiocin''' | ||
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==Reference== | ==Reference== | ||
DNA gyrase interaction with coumarin-based inhibitors: the role of the hydroxybenzoate isopentenyl moiety and the 5'-methyl group of the noviose., Lafitte D, Lamour V, Tsvetkov PO, Makarov AA, Klich M, Deprez P, Moras D, Briand C, Gilli R, Biochemistry. 2002 Jun 11;41(23):7217-23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12044152 12044152] | DNA gyrase interaction with coumarin-based inhibitors: the role of the hydroxybenzoate isopentenyl moiety and the 5'-methyl group of the noviose., Lafitte D, Lamour V, Tsvetkov PO, Makarov AA, Klich M, Deprez P, Moras D, Briand C, Gilli R, Biochemistry. 2002 Jun 11;41(23):7217-23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12044152 12044152] | ||
| - | [[Category: DNA topoisomerase (ATP-hydrolyzing)]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Moras, D.]] | [[Category: Moras, D.]] | ||
[[Category: Tsvetkov, P O.]] | [[Category: Tsvetkov, P O.]] | ||
| - | [[Category: | + | [[Category: Clorobiocin]] |
| - | [[Category: | + | [[Category: Gyrase b]] |
| - | [[Category: | + | [[Category: Topoisomerase]] |
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Revision as of 20:22, 2 May 2008
Crystal Structure of E. coli 24kDa Domain in Complex with Clorobiocin
Overview
DNA gyrase is a major bacterial protein that is involved in replication and transcription and catalyzes the negative supercoiling of bacterial circular DNA. DNA gyrase is a known target for antibacterial agents since its blocking induces bacterial death. Quinolones, coumarins, and cyclothialidines have been designed to inhibit gyrase. Significant improvements can still be envisioned for a better coumarin-gyrase interaction. In this work, we obtained the crystal costructures of the natural coumarin clorobiocin and a synthetic analogue with the 24 kDa gyrase fragment. We used isothermal titration microcalorimetry and differential scanning calorimetry to obtain the thermodynamic parameters representative of the molecular interactions occurring during the binding process between coumarins and the 24 kDa gyrase fragment. We provide the first experimental evidence that clorobiocin binds gyrase with a stronger affinity than novobiocin. We also demonstrate the crucial role of both the hydroxybenzoate isopentenyl moiety and the 5'-alkyl group on the noviose of the coumarins in the binding affinity for gyrase.
About this Structure
1KZN is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
DNA gyrase interaction with coumarin-based inhibitors: the role of the hydroxybenzoate isopentenyl moiety and the 5'-methyl group of the noviose., Lafitte D, Lamour V, Tsvetkov PO, Makarov AA, Klich M, Deprez P, Moras D, Briand C, Gilli R, Biochemistry. 2002 Jun 11;41(23):7217-23. PMID:12044152 Page seeded by OCA on Fri May 2 23:22:10 2008
