4oq2 | pdb_00004oq2

5hmC specific restriction endonuclease PvuRTs1I

spinqualitylabelsall models 4oq2, resolution 2.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4oq2 is a 1 chain structure with sequence from Atcc 29905. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: EPE NonStd Res: MSE Gene: 1239102, pvuRts1I (ATCC 29905) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed PvuRts1I is a prototype for a larger family of restriction endonucleases that cleave DNA containing 5-hydroxymethylcytosine (5hmC) or 5-glucosylhydroxymethylcytosine (5ghmC), but not 5-methylcytosine (5mC) or cytosine. Here, we report a crystal structure of the enzyme at 2.35 A resolution. Although the protein has been crystallized in the absence of DNA, the structure is very informative. It shows that PvuRts1I consists of an N-terminal, atypical PD-(D/E)XK catalytic domain and a C-terminal SRA domain that might accommodate a flipped 5hmC or 5ghmC base. Changes to predicted catalytic residues of the PD-(D/E)XK domain or to the putative pocket for a flipped base abolish catalytic activity. Surprisingly, fluorescence changes indicative of base flipping are not observed when PvuRts1I is added to DNA substrates containing pyrrolocytosine in place of 5hmC (5ghmC). Despite this caveat, the structure suggests a model for PvuRts1I activity and presents opportunities for protein engineering to alter the enzyme properties for biotechnological applications. Crystal structure of the 5hmC specific endonuclease PvuRts1I.,Kazrani AA, Kowalska M, Czapinska H, Bochtler M Nucleic Acids Res. 2014 Mar 25. PMID:24634440 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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