7MTT
Crystal structure of colibactin self-resistance protein ClbS in complex with two molecules of CHES
Summary for 7MTT
| Entry DOI | 10.2210/pdb7mtt/pdb |
| Descriptor | Colibactin self-protection protein ClbS, 2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID (3 entities in total) |
| Functional Keywords | hydrolase, dna repair, dna binding protein |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 21162.24 |
| Authors | Tripathi, P.,Bruner, S.D. (deposition date: 2021-05-13, release date: 2021-05-26, Last modification date: 2023-10-18) |
| Primary citation | Tripathi, P.,Bruner, S.D. Structural Basis for the Interactions of the Colibactin Resistance Gene Product ClbS with DNA. Biochemistry, 60:1619-1625, 2021 Cited by PubMed Abstract: The natural product colibactin, along with its associated biosynthetic gene cluster, is an example system for the role microbially derived small molecules play in the human microbiome. This is particularly relevant in the human gut, where host microbiota is involved in various disorders, including colorectal cancer pathogenesis. Bacteria harboring the colibactin gene cluster induce alkylation of nucleobases in host DNA, forming interstrand cross-links both and . These lesions can lead to deleterious double-strand breaks and have been identified as the primary mechanism of colibactin-induced cytotoxicity. The gene product ClbS is one of several mechanisms utilized by the producing bacteria to maintain genome integrity. ClbS catalyzes hydrolytic inactivation of colibactin and has been shown to bind DNA, incurring self-resistance. Presented is the molecular basis for ClbS bound to a DNA oligonucleotide. The structure shows the interaction of the protein with the ends of a DNA duplex with terminal nucleotides flipped to the enzyme active site. The structure suggests an additional function for ClbS, the binding to damaged DNA followed by repair. Additionally, our study provides general insight into the function of the widely distributed and largely uncharacterized DUF1706 protein family. PubMed: 33945270DOI: 10.1021/acs.biochem.1c00201 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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