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- W2000720921 abstract "Sequence-specific interactions between proteins and DNA are essential for a variety of biological functions. The (cytosine-C5)-methyltransferase from HhaI (M.HhaI) specifically modifies the second base in GCGC sequences, employing a base flipping mechanism to access the target base being chemically modified. The mechanism of sequence-specific recognition of M.HhaI is not evident based on crystallographic structures, leading to the suggestion that recognition is linked to the flipping event itself, a process that may be referred to as energetic recognition. Using computational methods, it is shown that the free energy barriers to flipping are significantly higher in non-cognate versus the cognate sequence, supporting the energetic recognition mechanism. Energetic recognition is imparted by two protein “selectivity filters” that function via a “web” of protein–DNA interactions in short-lived, high energy states present along the base flipping pathway. Other sequence-specific DNA binding proteins whose function involves significant distortion of DNA's conformation may use a similar recognition mechanism." @default.
- W2000720921 created "2016-06-24" @default.
- W2000720921 creator A5056944006 @default.
- W2000720921 creator A5074665620 @default.
- W2000720921 date "2005-01-01" @default.
- W2000720921 modified "2023-09-26" @default.
- W2000720921 title "Specificity in Protein–DNA Interactions: Energetic Recognition by the (Cytosine-C5)-methyltransferase from HhaI" @default.
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- W2000720921 doi "https://doi.org/10.1016/j.jmb.2004.10.042" @default.
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