2ixs | pdb_00002ixs

Structure of SdaI restriction endonuclease

spinqualitylabelsall models 2ixs, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2ixs is a 2 chain structure with sequence from "actinomyces_diastaticus"_krainsky_1914 "actinomyces diastaticus" krainsky 1914. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: EPE, SO4, TRS Activity: Type II site-specific deoxyribonuclease, with EC number 3.1.21.4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Rare-cutting restriction enzymes are important tools in genome analysis. We report here the crystal structure of SdaI restriction endonuclease, which is specific for the 8 bp sequence CCTGCA/GG ("/" designates the cleavage site). Unlike orthodox Type IIP enzymes, which are single domain proteins, the SdaI monomer is composed of two structural domains. The N domain contains a classical winged helix-turn-helix (wHTH) DNA binding motif, while the C domain shows a typical restriction endonuclease fold. The active site of SdaI is located within the C domain and represents a variant of the canonical PD-(D/E)XK motif. SdaI determinants of sequence specificity are clustered on the recognition helix of the wHTH motif at the N domain. The modular architecture of SdaI, wherein one domain mediates DNA binding while the other domain is predicted to catalyze hydrolysis, distinguishes SdaI from previously characterized restriction enzymes interacting with symmetric recognition sequences. The crystal structure of the rare-cutting restriction enzyme SdaI reveals unexpected domain architecture.,Tamulaitiene G, Jakubauskas A, Urbanke C, Huber R, Grazulis S, Siksnys V Structure. 2006 Sep;14(9):1389-400. PMID:16962970 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Endonuclease

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