3EDC

Crystal Structure of a 1.6-hexanediol Bound Tetrameric Form of Escherichia coli Lac-repressor Refined to 2.1 Resolution

3EDC の概要

• エントリーDOI: 10.2210/pdb3edc/pdb
• 分子名称: Lactose operon repressor, HEXANE-1,6-DIOL (3 entities in total)
• 機能のキーワード: lac-repressor, allosteric, tetramer, dna-binding, repressor, transcription, transcription regulation
• 由来する生物種: Escherichia coli K12
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 154980.79

構造登録者

Stenberg, K.A.E. (登録日: 2008-09-03, 公開日: 2008-11-25, 最終更新日: 2023-11-01)

主引用文献

Stenberg, K.A.E.,Vihinen, M.
Crystal structure of a 1.6-hexanediol bound tetrameric form of Escherichia coli lac-repressor refined to 2.1 A resolution
Proteins, 75:748-759, 2009

PubMed Abstract: We report the structure of a novel tetrameric form of the lactose repressor (LacI) protein from Escherichia coli refined to 2.1 A resolution. The tetramer is bound to 1.6-hexanediol present in the crystallization solution and the final R(free) for the structure is 0.201. The structure confirms previously reported structures on the monomer level. However, the tetramer is much more densely packed. This adds a new level of complexity to the interpretation of mutational effects and challenges details in the current model for LacI function. Several amino acids, previously associated with changes in function but unexplained at the structural level, appear in a new structural context in this tetramer which provides new implications for their function.

PubMed: 19004002
DOI: 10.1002/prot.22284

実験手法

X-RAY DIFFRACTION (2.1 Å)