5akm

THE CRYSTAL STRUCTURE OF I-DMOI G20S IN COMPLEX WITH ITS TARGET DNA IN THE PRESENCE OF 2MM MG

spinqualitylabelsall models 5akm, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5akm is a 15 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACT, MG Related: 5ak9, 5akf, 5akn Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [DMO1_DESMO] Endonuclease involved in intron homing. Recognizes a recognizes up to 20 bp of DNA in the 23S rRNA gene intron. It has a slow turnover rate and cuts the coding strand with a slight preference over the non-coding strand. Publication Abstract from PubMed Homing endonucleases are useful tools for genome modification due to their capability to recognize and cleave specifically large DNA targets. These endonucleases generate a DNA double-strand break that can be repaired by the DNA damage response machinery. The break can be repaired by homologous recombination, an error-free mechanism, or by non-homologous end joining, a process susceptible to introduce errors in the repaired sequence. The type of DNA cleavage might alter the balance between these two alternatives. The use of nickases producing a specific single strand break instead of a double-strand break could be an approach to reduce the toxicity associated to non-homologous end joining by promoting the use of homologous recombination to repair the cleavage of a single DNA break. Taking advantage of the sequential DNA cleavage mechanism of I-DmoI LAGLIDADG homing endonuclease we have developed a new variant that is able to cut preferentially the coding DNA strand generating a nicked DNA target. Our structural and biochemical analysis shows that by decoupling the action of the catalytic residues acting on each strand, we can inhibit one of them while keeping the other functional. Engineering a nickase on the homing endonuclease I-DmoI scaffold.,Molina R, Marcaida MJ, Redondo P, Marenchino M, Duchateau P, D'Abramo M, Montoya G, Prieto J J Biol Chem. 2015 Jun 4. pii: jbc.M115.658666. PMID:26045557 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Endonuclease 3D structures

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