2nov
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(New page: 200px<br /><applet load="2nov" size="450" color="white" frame="true" align="right" spinBox="true" caption="2nov, resolution 2.67Å" /> '''Breakage-reunion dom...)
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Revision as of 10:42, 21 November 2007
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Breakage-reunion domain of S.pneumoniae topo IV: crystal structure of a gram-positive quinolone target
Overview
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.
About this Structure
2NOV is a Single protein structure of sequence from Streptococcus pneumoniae. Full crystallographic information is available from OCA.
Reference
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, PLoS ONE. 2007 Mar 21;2:e301. PMID:17375187
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