6h2j | pdb_00006h2j

Crystal structure of the HsdR subunit of the EcoR124I restriction enzyme with the C-terminal domain

spinqualitylabelsall models 6h2j, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6h2j is a 2 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ATP, MG NonStd Res: MSE Related: 2w00, 5j3n Gene: hsdR ("Bacillus coli" Migula 1895) Activity: Type I site-specific deoxyribonuclease, with EC number 3.1.21.3 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Although EcoR124 is one of the better-studied Type I restriction-modification enzymes, it still presents many challenges to detailed analyses because of its structural and functional complexity and missing structural information. In all available structures of its motor subunit HsdR, responsible for DNA translocation and cleavage, a large part of the HsdR C terminus remains unresolved. The crystal structure of the C terminus of HsdR, obtained with a crystallization chaperone in the form of pHluorin fusion and refined to 2.45 A, revealed that this part of the protein forms an independent domain with its own hydrophobic core and displays a unique alpha-helical fold. The full-length HsdR model, based on the wild-type structure and the herein determined C-terminal domain, disclosed a proposed DNA-binding groove lined by positively charged residues. In vivo and in vitro assays with a C-terminal deletion mutant of HsdR supported the idea that this domain is involved in complex assembly and DNA binding. Conserved residues identified through sequence analysis of the C-terminal domain may play a key role in protein-protein and protein-DNA interactions. We conclude that the motor subunit of EcoR124 comprises five structural and functional domains, with the fifth, C-terminal domain revealing a unique fold characterized by four conserved motifs in the IC subfamily of Type I restriction-modification systems. In summary, structural and biochemical results reported here support a model in which the C-terminal domain of the motor subunit HsdR of the endonuclease EcoR124 is involved in complex assembly and DNA binding. Crystal structure of a novel domain of the motor subunit of the Type I restriction enzyme EcoR124 involved in complex assembly and DNA binding.,Grinkevich P, Sinha D, Iermak I, Guzanova A, Weiserova M, Ludwig J, Mesters JR, Ettrich RH J Biol Chem. 2018 Jul 27. pii: RA118.003978. doi: 10.1074/jbc.RA118.003978. PMID:30054276 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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