IRUS Total

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

Title: Breakage-Reunion Domain of Streptococcus pneumoniae Topoisomerase IV: Crystal Structure of a Gram-Positive Quinolone Target
Authors: Laponogov, I
Veselkov, DA
Sohi, MK
Pan, XS
Achari, A
Yang, C
Ferrara, JD
Fisher, LM
Sanderson, MR
Item Type: Journal Article
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.
Issue Date: 21-Mar-2007
Date of Acceptance: 21-Feb-2007
URI: http://hdl.handle.net/10044/1/38506
DOI: http://dx.doi.org/10.1371/journal.pone.0000301
ISSN: 1932-6203
Publisher: Public Library of Science
Journal / Book Title: PLOS One
Volume: 2
Issue: 3
Copyright Statement: 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
Escherichia coli
Protein Conformation
Static Electricity
Streptococcus pneumoniae
General Science & Technology
MD Multidisciplinary
Publication Status: Published
Article Number: e301
Appears in Collections:Department of Surgery and Cancer