8E9A
Crystal structure of AsfvPolX in complex with 10-23 DNAzyme and Mg
Summary for 8E9A
| Entry DOI | 10.2210/pdb8e9a/pdb |
| Descriptor | Repair DNA polymerase X, DNA/RNA (52-MER), MAGNESIUM ION, ... (5 entities in total) |
| Functional Keywords | dnazyme, dna, transferase-dna complex, transferase/dna |
| Biological source | African swine fever virus BA71V More |
| Total number of polymer chains | 4 |
| Total formula weight | 73503.55 |
| Authors | Cramer, E.R.,Robart, A.R.,Kaya, A.I. (deposition date: 2022-08-26, release date: 2023-06-21, Last modification date: 2024-10-09) |
| Primary citation | Cramer, E.R.,Starcovic, S.A.,Avey, R.M.,Kaya, A.I.,Robart, A.R. Structure of a 10-23 deoxyribozyme exhibiting a homodimer conformation. Commun Chem, 6:119-119, 2023 Cited by PubMed Abstract: Deoxyribozymes (DNAzymes) are in vitro evolved DNA sequences capable of catalyzing chemical reactions. The RNA-cleaving 10-23 DNAzyme was the first DNAzyme to be evolved and possesses clinical and biotechnical applications as a biosensor and a knockdown agent. DNAzymes do not require the recruitment of other components to cleave RNA and can turnover, thus they have a distinct advantage over other knockdown methods (siRNA, CRISPR, morpholinos). Despite this, a lack of structural and mechanistic information has hindered the optimization and application of the 10-23 DNAzyme. Here, we report a 2.7 Å crystal structure of the RNA-cleaving 10-23 DNAzyme in a homodimer conformation. Although proper coordination of the DNAzyme to substrate is observed along with intriguing patterns of bound magnesium ions, the dimer conformation likely does not capture the true catalytic form of the 10-23 DNAzyme. PubMed: 37301907DOI: 10.1038/s42004-023-00924-3 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.69 Å) |
Structure validation
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