Domain Swapping in Allosteric Modulation of DNA Specificity
Author(s) -
Chad K. Park,
Hemant Joshi,
Alka Agrawal,
M. Imran Ghare,
E.J. Little,
Pete Dunten,
Jurate Bitinaite,
Nancy C. Horton
Publication year - 2010
Publication title -
plos biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.127
H-Index - 271
eISSN - 1545-7885
pISSN - 1544-9173
DOI - 10.1371/journal.pbio.1000554
Subject(s) - tetramer , allosteric regulation , dna , biology , restriction enzyme , cleavage (geology) , dimer , endonuclease , protein–dna interaction , dna clamp , biophysics , stereochemistry , biochemistry , enzyme , dna binding protein , chemistry , transcription factor , gene , rna , organic chemistry , fracture (geology) , paleontology , reverse transcriptase
The structure of two DNA-bound SgrAI enzyme dimers is presented, along with mutagenesis experiments supporting a role for this structure in polymer formation and the activation of DNA cleavage by SgrAI.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom