4z20

Crystal Structure of Meganuclease I-SmaMI Bound to Uncleaveable DNA with a TTGT Central Four

spinqualitylabelsall models 4z20, resolution 3.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4z20 is a 6 chain structure with sequence from Sordaria macrospora k-hell and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.2Å Ligands: CA, GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function F7WD42_SORMK Publication Abstract from PubMed LAGLIDADG meganucleases are DNA cleaving enzymes used for genome engineering. While their cleavage specificity can be altered using several protein engineering and selection strategies, their overall targetability is limited by highly specific indirect recognition of the central four base pairs within their recognition sites. In order to examine the physical basis of indirect sequence recognition and to expand the number of such nucleases available for genome engineering, we have determined the target sites, DNA-bound structures, and central four cleavage fidelities of nine related enzymes. Subsequent crystallographic analyses of a meganuclease bound to two noncleavable target sites, each containing a single inactivating base pair substitution at its center, indicates that a localized slip of the mutated base pair causes a small change in the DNA backbone conformation that results in a loss of metal occupancy at one binding site, eliminating cleavage activity. Indirect DNA Sequence Recognition and Its Impact on Nuclease Cleavage Activity.,Lambert AR, Hallinan JP, Shen BW, Chik JK, Bolduc JM, Kulshina N, Robins LI, Kaiser BK, Jarjour J, Havens K, Scharenberg AM, Stoddard BL Structure. 2016 Apr 27. pii: S0969-2126(16)30035-1. doi:, 10.1016/j.str.2016.03.024. PMID:27133026 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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