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Structure and properties of a truely apo form of AraC dimerization domain
Author(s) -
Weldon John E.,
Rodgers Michael E.,
Larkin Christopher,
Schleif Robert F.
Publication year - 2006
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.21267
Subject(s) - chemistry , monomer , mutant , arabinose , protein structure , fucose , plasma protein binding , biophysics , domain (mathematical analysis) , crystallography , protein domain , side chain , glycoprotein , biochemistry , biology , organic chemistry , mathematical analysis , mathematics , xylose , fermentation , gene , polymer
The arabinose‐binding pockets of wild type AraC dimerization domains crystallized in the absence of arabinose are occupied with the side chains of Y31 from neighboring domains. This interaction leads to aggregation at high solution concentrations and prevents determination of the structure of truely apo AraC. In this work we found that the aggregation does not significantly occur at physiological concentrations of AraC. We also found that the Y31V mutation eliminates the self‐association, but does not affect regulation properties of the protein. At the same time, the mutation allows crystallization of the dimerization domain of the protein with only solvent in the arabinose‐binding pocket. Using a distance difference method suitable for detecting and displaying even minor structural variation among large groups of similar structures, we find that there is no significant structural change in the core of monomers of the AraC dimerization domain resulting from arabinose, fucose, or tyrosine occupancy of the ligand‐binding pocket. A slight change is observed in the relative orientation of monomers in the dimeric form of the domain upon the binding of arabinose but its significance cannot yet be assessed. Proteins 2007. © 2006 Wiley‐Liss, Inc.