5o6g

Structures and dynamics of mesophilic variants from the homing endonuclease I-DmoI

spinqualitylabelsall models 5o6g, resolution 2.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5o6g is a 9 chain structure with sequence from Desulfurococcus mucosus 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 2.75Å Ligands: CL, MN 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 I-DmoI, from the hyperthermophilic archaeon Desulfurococcus mobilis, belongs to the LAGLIDADG homing endonuclease protein family. Its members are highly specific enzymes capable of recognizing long DNA target sequences, thus providing potential tools for genome manipulation. Working towards this particular application, many efforts have been made to generate mesophilic variants of I-DmoI that function at lower temperatures than the wild-type. Here, we report a structural and computational analysis of two I-DmoI mesophilic mutants. Despite very limited structural variations between the crystal structures of these variants and the wild-type, a different dynamical behaviour near the cleavage sites is observed. In particular, both the dynamics of the water molecules and the protein perturbation effect on the cleavage site correlate well with the changes observed in the experimental enzymatic activity. Structure and dynamics of mesophilic variants from the homing endonuclease I-DmoI.,Alba J, Marcaida MJ, Prieto J, Montoya G, Molina R, D'Abramo M J Comput Aided Mol Des. 2017 Nov 25. pii: 10.1007/s10822-017-0087-5. doi:, 10.1007/s10822-017-0087-5. PMID:29177929 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Endonuclease 3D structures

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