4aae | pdb_00004aae

Crystal structure of the mutant D75N I-CreI in complex with an altered target (The four central bases, 2NN region, are composed by AGCG from 5' to 3')

spinqualitylabelsall models 4aae, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4aae is a 4 chain structure with sequence from Chlre. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1g9z, 1bp7, 1af5, 2vbl, 2vbj, 2vbo, 1mow, 1g9y, 1n3f, 2vbn, 1u0d, 1t9i, 1t9j, 1n3e, 1u0c, 4aaf, 4aag, 4aad, 4aab Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [DNE1_CHLRE] Endonuclease involved in group I intron homing. Recognizes and cleaves a 19-24 bp palindromic DNA site. Publication Abstract from PubMed Homing endonucleases represent protein scaffolds that provide powerful tools for genome manipulation, as these enzymes possess a very low frequency of DNA cleavage in eukaryotic genomes due to their high specificity. The basis of protein-DNA recognition must be understood to generate tailored enzymes that target the DNA at sites of interest. Protein-DNA interaction engineering of homing endonucleases has demonstrated the potential of these approaches to create new specific instruments to target genes for inactivation or repair. Protein-DNA interface studies have been focused mostly on specific contacts between amino acid side chains and bases to redesign the binding interface. However, it has been shown that 4 bp in the central DNA sequence of the 22-bp substrate of a homing endonuclease (I-CreI), which do not show specific protein-DNA interactions, is not devoid of content information. Here, we analyze the mechanism of target discrimination in this substrate region by the I-CreI protein, determining how it can occur independently of the specific protein-DNA interactions. Our data suggest the important role of indirect readout in this substrate region, opening the possibility for a fully rational search of new target sequences, thus improving the development of redesigned enzymes for therapeutic and biotechnological applications. Non-specific protein-DNA interactions control I-CreI target binding and cleavage.,Molina R, Redondo P, Stella S, Marenchino M, D'Abramo M, Gervasio FL, Charles Epinat J, Valton J, Grizot S, Duchateau P, Prieto J, Montoya G Nucleic Acids Res. 2012 Apr 11. PMID:22495931 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Endonuclease 3D structures

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