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• W2044145557 abstract "Among four types of bacterial restriction enzymes that cleave a foreign DNA depending on its methylation status, type I enzymes composed of three subunits are interesting because of their unique DNA cleavage and translocation mechanisms performed by the restriction subunit (HsdR). The elucidated N-terminal fragment structure of a putative HsdR subunit from Vibrio vulnificus YJ016 reveals three globular domains. The nucleolytic core within an N-terminal nuclease domain (NTD) is composed of one basic and three acidic residues, which include a metal-binding site. An ATP hydrolase (ATPase) site at the interface of two RecA-like domains (RDs) is located close to the probable DNA-binding site for translocation, which is far from the NTD nucleolytic core. Comparison of relative domain arrangements with other functionally related ATP and/or DNA complex structures suggests a possible translocation and restriction mechanism of the HsdR subunit. Furthermore, careful analysis of its sequence and structure implies that a linker helix connecting two RDs and an extended region within the nuclease domain may play a central role in switching the DNA translocation into the restriction activity." @default.
• W2044145557 created "2016-06-24" @default.
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• W2044145557 date "2009-07-22" @default.
• W2044145557 modified "2023-09-27" @default.
• W2044145557 title "The fragment structure of a putative HsdR subunit of a type I restriction enzyme from Vibrio vulnificus YJ016: implications for DNA restriction and translocation activity" @default.
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• W2044145557 doi "https://doi.org/10.1093/nar/gkp603" @default.
• W2044145557 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2777439" @default.
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• W2044145557 hasPublicationYear "2009" @default.
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