Ontology highlight
ABSTRACT:
SUBMITTER: Laponogov I
PROVIDER: S-EPMC1810434 | biostudies-literature | 2007 Mar
REPOSITORIES: biostudies-literature
Laponogov Ivan I Veselkov Dennis A DA Sohi Maninder K MK Pan Xiao-Su XS Achari Aniruddha A Yang Cheng C Ferrara Joseph D JD Fisher L Mark LM Sanderson Mark R MR
PloS one 20070321 3
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 exh ...[more]