6rks

E. coli DNA Gyrase - DNA binding and cleavage domain in State 1 without TOPRIM insertionE. coli DNA Gyrase - DNA binding and cleavage domain in State 1 without TOPRIM insertion

6rks, resolution 4.00Å Show:Asymmetric Unit Biological Assembly Structural highlights 6rks is a 8 chain structure with sequence from Ecoli and Escherichia coli o157:h7 str. ss52. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: Gene: gyrA, hisW, nalA, parD, b2231, JW2225 (ECOLI), gyrB, acrB, cou, himB, hisU, nalC, parA, pcbA, b3699, JW5625 (Escherichia coli O157:H7 str. SS52) Activity: DNA topoisomerase, with EC number 5.6.2.2 Experimental data: Check Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [GYRA_ECOLI] DNA gyrase negatively supercoils closed circular double-stranded DNA in an ATP-dependent manner and also catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes and knotted rings. [GYRB_ECOLI] DNA gyrase negatively supercoils closed circular double-stranded DNA in an ATP-dependent manner and also catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes and knotted rings. Publication Abstract from PubMed DNA gyrase is an essential enzyme involved in the homeostatic control of DNA supercoiling and the target of successful antibacterial compounds. Despite extensive studies, a detailed architecture of the full-length DNA gyrase from the model organism E. coli is still missing. Herein, we report the complete structure of the E. coli DNA gyrase nucleoprotein complex trapped by the antibiotic gepotidacin, using phase-plate single-particle cryo-electron microscopy. Our data unveil the structural and spatial organization of the functional domains, their connections and the position of the conserved GyrA-box motif. The deconvolution of two states of the DNA-binding/cleavage domain provides a better understanding of the allosteric movements of the enzyme complex. The local atomic resolution in the DNA-bound area reaching up to 3.0 A enables the identification of the antibiotic density. Altogether, this study paves the way for the cryo-EM determination of gyrase complexes with antibiotics and opens perspectives for targeting conformational intermediates. Cryo-EM structure of the complete E. coli DNA gyrase nucleoprotein complex.,Vanden Broeck A, Lotz C, Ortiz J, Lamour V Nat Commun. 2019 Oct 30;10(1):4935. doi: 10.1038/s41467-019-12914-y. PMID:31666516 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Topoisomerase 3D structures