1XJA

Apo form of the Y31V mutant dimerization domain fragment of Escherichia coli regulatory protein AraC

1XJA の概要

• エントリーDOI: 10.2210/pdb1xja/pdb
• 関連するPDBエントリー: 2AAC 2ARA 2ARC 2K9S
• 分子名称: Arabinose operon regulatory protein, 1,2-ETHANEDIOL (3 entities in total)
• 機能のキーワード: transcription factor, coiled-coil, jelly roll, allostery, arabinose, carbohydrate binding, arac, transcription
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm: P0A9E0
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 104623.40

構造登録者

Weldon, J.E.,Larkin, C.,Schleif, R.F. (登録日: 2004-09-23, 公開日: 2004-10-12, 最終更新日: 2023-08-23)

主引用文献

Weldon, J.E.,Rodgers, M.E.,Larkin, C.,Schleif, R.F.
Structure and properties of a truely apo form of AraC dimerization domain.
Proteins, 66:646-654, 2007

PubMed Abstract: 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.

PubMed: 17173282
DOI: 10.1002/prot.21267

実験手法

X-RAY DIFFRACTION (2.4 Å)