2NOV

Breakage-reunion domain of S.pneumoniae topo IV: crystal structure of a gram-positive quinolone target

2NOV の概要

• エントリーDOI: 10.2210/pdb2nov/pdb
• 分子名称: DNA topoisomerase 4 subunit A (2 entities in total)
• 機能のキーワード: protein, parc, topo iv, gram-positive bacteria, quinolone target, dna binding, dna cleavage, isomerase
• 由来する生物種: Streptococcus pneumoniae
• 細胞内の位置: Cell membrane ; Peripheral membrane protein : P72525
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 225821.74

構造登録者

Laponogov, I.,Veselkov, D.A.,Sohi, M.K.,Pan, X.S.,Achari, A.,Yang, C.,Ferrara, J.D.,Fisher, L.M.,Sanderson, M.R. (登録日: 2006-10-26, 公開日: 2006-11-14, 最終更新日: 2023-08-30)

主引用文献

Laponogov, I.,Veselkov, D.A.,Sohi, M.K.,Pan, X.S.,Achari, A.,Yang, C.,Ferrara, J.D.,Fisher, L.M.,Sanderson, M.R.
Breakage-Reunion Domain of Streptococcus pneumoniae Topoisomerase IV: Crystal Structure of a Gram-Positive Quinolone Target.
PLoS ONE, 2:e301-e301, 2007

PubMed 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.

PubMed: 17375187
DOI: 10.1371/journal.pone.0000301

実験手法

X-RAY DIFFRACTION (2.67 Å)