6HPC
Crystal structure of the HicB antitoxin from E. coli
Summary for 6HPC
| Entry DOI | 10.2210/pdb6hpc/pdb |
| Related | 6HPB |
| Descriptor | Antitoxin HicB (2 entities in total) |
| Functional Keywords | dna binding, helix-turn-helix, hth, antitoxin |
| Biological source | Escherichia coli 2-210-07_S3_C3 |
| Total number of polymer chains | 2 |
| Total formula weight | 30898.27 |
| Authors | Manav, M.C.,Brodersen, D.E. (deposition date: 2018-09-20, release date: 2019-09-18, Last modification date: 2024-10-16) |
| Primary citation | Manav, M.C.,Turnbull, K.J.,Jurenas, D.,Garcia-Pino, A.,Gerdes, K.,Brodersen, D.E. The E. coli HicB Antitoxin Contains a Structurally Stable Helix-Turn-Helix DNA Binding Domain. Structure, 27:1675-1685.e3, 2019 Cited by PubMed Abstract: The E. coli hicAB type II toxin-antitoxin locus is unusual by being controlled by two promoters and by having the toxin encoded upstream of the antitoxin. HicA toxins contain a double-stranded RNA-binding fold and cleaves both mRNA and tmRNA in vivo, while HicB antitoxins contain a partial RNase H fold and either a helix-turn-helix (HTH) or ribbon-helix-helix domain. It is not known how an HTH DNA-binding domain affects higher-order structure for the HicAB modules. Here, we present crystal structures of the isolated E. coli HicB antitoxin and full-length HicAB complex showing that HicB forms a stable DNA-binding module and interacts in a canonical way with HicA despite the presence of an HTH-type DNA-binding domain. No major structural rearrangements take place upon binding of the toxin. Both structures expose well-ordered DNA-binding motifs allowing a model for DNA binding by the antitoxin to be generated. PubMed: 31495532DOI: 10.1016/j.str.2019.08.008 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.26 Å) |
Structure validation
Download full validation report
