1X75

CcdB:GyrA14 complex

Summary for 1X75

• Entry DOI: 10.2210/pdb1x75/pdb
• Related: 1ab4 1vub 2vub 3vub 4vub
• Descriptor: DNA gyrase subunit A, Cytotoxic protein ccdB (3 entities in total)
• Functional Keywords: gyrase, ccdb, topoisomerase, plasmid addiction, ta system, bacterial cell death, isomerase-signaling protein complex, isomerase/signaling protein
• Biological source: Escherichia coli; More
• Cellular location: Cytoplasm (Potential): P09097
• Total number of polymer chains: 4
• Total formula weight: 53285.21

Authors

Dao-Thi, M.H.,Van Melderen, L.,De Genst, E.,Wyns, L.,Loris, R. (deposition date: 2004-08-13, release date: 2005-05-17, Last modification date: 2024-03-13)

Primary citation

Dao-Thi, M.H.,Van Melderen, L.,De Genst, E.,Afif, H.,Buts, L.,Wyns, L.,Loris, R.
Molecular Basis of Gyrase Poisoning by the Addiction Toxin CcdB
J.Mol.Biol., 348:1091-1102, 2005

PubMed Abstract: Gyrase is an ubiquitous bacterial enzyme that is responsible for disentangling DNA during DNA replication and transcription. It is the target of the toxin CcdB, a paradigm for plasmid addiction systems and related bacterial toxin-antitoxin systems. The crystal structure of CcdB and the dimerization domain of the A subunit of gyrase (GyrA14) dictates an open conformation for the catalytic domain of gyrase when CcdB is bound. The action of CcdB is one of a wedge that stabilizes a dead-end covalent gyrase:DNA adduct. Although CcdB and GyrA14 form a globally symmetric complex where the two 2-fold axes of both dimers align, the complex is asymmetric in its details. At the centre of the interaction site, the Trp99 pair of CcdB stacks with the Arg462 pair of GyrA14, explaining why the Arg462Cys mutation in the A subunit of gyrase confers resistance to CcdB. Overexpression of GyrA14 protects Escherichia coli cells against CcdB, mimicking the action of the antidote CcdA.

PubMed: 15854646
DOI: 10.1016/j.jmb.2005.03.049

Experimental method

X-RAY DIFFRACTION (2.8 Å)