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Breakage-Reunion Domain of Streptococcus pneumoniae Topoisomerase IV: Crystal Structure of a Gram-Positive Quinolone Target.

Laponogov, I; Veselkov, DA; Sohi, MK; Pan, XS; Achari, A; Yang, C; Ferrara, JD; Fisher, LM; Sanderson, MR (2007) Breakage-Reunion Domain of Streptococcus pneumoniae Topoisomerase IV: Crystal Structure of a Gram-Positive Quinolone Target. PLOS ONE, 2 (3). e301. ISSN 1932-6203 https://doi.org/10.1371/journal.pone.0000301
SGUL Authors: Fisher, Larry Mark Laponogov, Ivan

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Abstract

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.

Item Type: Article
Additional Information: PubMed ID: 17375187. This is an open-access article distributed under the terms of the Creative Commons Public Domain declaration which stipulates that, once placed in the public domain, this work may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose.
Keywords: Binding Sites, Crystallography, X-Ray, DNA Topoisomerase IV, DNA Topoisomerases, Type II, DNA, Bacterial, Dimerization, Escherichia coli, Protein Conformation, Quinolones, Static Electricity, Streptococcus pneumoniae, Science & Technology, Multidisciplinary Sciences, Science & Technology - Other Topics
SGUL Research Institute / Research Centre: Academic Structure > Molecular and Clinical Sciences Research Institute (MCS)
Academic Structure > Molecular and Clinical Sciences Research Institute (MCS) > Cell Sciences (INCCCS)
Journal or Publication Title: PLOS ONE
ISSN: 1932-6203
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Dates:
DateEvent
21 March 2007Published
Web of Science ID: WOS:000207445100003
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URI: http://openaccess.sgul.ac.uk/id/eprint/552
Publisher's version: https://doi.org/10.1371/journal.pone.0000301

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