Breakage-Reunion Domain of Streptococcus pneumoniae Topoisomerase IV: Crystal Structure of a Gram-Positive Quinolone Target
Autor: | Aniruddha Achari, M.K. Sohi, X.-S. Pan, D.A. Veselkov, Ivan Laponogov, Joseph D. Ferrara, Mark R. Sanderson, L. Mark Fisher, Cheng Yang |
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Rok vydání: | 2007 |
Předmět: |
DNA Topoisomerase IV
DNA Bacterial medicine.drug_class Topoisomerase IV Stereochemistry Protein Conformation General Science & Technology Science Static Electricity Biophysics Computational Biology/Macromolecular Structure Analysis Quinolones medicine.disease_cause Crystallography X-Ray DNA gyrase chemistry.chemical_compound MD Multidisciplinary medicine Escherichia coli Biochemistry/Macromolecular Chemistry Binding site Multidisciplinary Binding Sites biology Topoisomerase biochemical phenomena metabolism and nutrition Quinolone DNA binding site DNA Topoisomerases Type II Streptococcus pneumoniae Biochemistry chemistry biology.protein Medicine bacteria Biophysics/Biomacromolecule-Ligand Interactions Dimerization DNA Research Article |
Zdroj: | PLoS ONE PLoS ONE, Vol 2, Iss 3, p e301 (2007) |
ISSN: | 1932-6203 |
Popis: | The 2.7 A crystal structure of the 55-kDa N-terminal breakage-reunion domain of topoisomerase (topo) IV subunit A (ParC) from Streptococcus pneumoniae, the first for the quinolone targets from a gram-positive bacterium, has been solved and reveals a 'closed' dimer similar in fold to Escherichia coli DNA gyrase subunit A (GyrA), but distinct from the 'open' gate structure of Escherichia coli ParC. Unlike GyrA whose DNA binding groove is largely positively charged, the DNA binding site of ParC exhibits a distinct pattern of alternating positively and negatively charged regions coincident with the predicted positions of the grooves and phosphate backbone of DNA. Based on the ParC structure, a new induced-fit model for sequence-specific recognition of the gate (G) segment by ParC has been proposed. These features may account for the unique DNA recognition and quinolone targeting properties of pneumococcal type II topoisomerases compared to their gram-negative counterparts. |
Databáze: | OpenAIRE |
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