2GQQ

Crystal Structure of E. coli Leucine-responsive regulatory protein (Lrp)

2GQQ の概要

• エントリーDOI: 10.2210/pdb2gqq/pdb
• 分子名称: Leucine-responsive regulatory protein (1 entity in total)
• 機能のキーワード: helix-turn-helix, transcription
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 75134.40

構造登録者

de los Rios, S.,Perona, J.J. (登録日: 2006-04-21, 公開日: 2007-03-06, 最終更新日: 2024-02-14)

主引用文献

de Los Rios, S.,Perona, J.J.
Structure of the Escherichia coli Leucine-responsive Regulatory Protein Lrp Reveals a Novel Octameric Assembly.
J.Mol.Biol., 366:1589-1602, 2007

PubMed Abstract: The structure of Escherichia coli leucine-responsive regulatory protein (Lrp) co-crystallized with a short duplex oligodeoxynucleotide reveals a novel quaternary assembly in which the protein octamer forms an open, linear array of four dimers. In contrast, structures of the Lrp homologs LrpA, LrpC and AsnC crystallized in the absence of DNA show that these proteins instead form highly symmetrical octamers in which the four dimers form a closed ring. Although the DNA is disordered within the Lrp crystal, comparative analyses suggest that the observed differences in quaternary state may arise from DNA interactions during crystallization. Interconversion of these conformations, possibly in response to DNA or leucine binding, provides an underlying mechanism to alter the relative spatial orientation of the DNA-binding domains. Breaking of the closed octamer symmetry may be a common essential step in the formation of active DNA complexes by all members of the Lrp/AsnC family of transcriptional regulatory proteins.

PubMed: 17223133
DOI: 10.1016/j.jmb.2006.12.032

実験手法

X-RAY DIFFRACTION (3.2 Å)