2FYM

Crystal structure of E. coli enolase complexed with the minimal binding segment of RNase E.

2FYM の概要

• エントリーDOI: 10.2210/pdb2fym/pdb
• 関連するPDBエントリー: 1E9I
• 分子名称: Enolase, Ribonuclease E, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: rna degradosome, enolase, rnase e, lyase
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Cytoplasm, cytoskeleton: P0A6P9; Cytoplasm : P21513
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 186502.50

構造登録者

Chandran, V.,Luisi, B.F. (登録日: 2006-02-08, 公開日: 2006-02-28, 最終更新日: 2023-08-30)

主引用文献

Chandran, V.,Luisi, B.F.
Recognition of Enolase in the Escherichia coli RNA Degradosome
J.Mol.Biol., 358:8-15, 2006

PubMed Abstract: In Escherichia coli, the glycolytic enzyme enolase is a component of the RNA degradosome, which is an RNase E mediated assembly involved in RNA processing and transcript turnover. The recruitment of enolase by the RNA degradosome has been implicated in the turnover of certain transcripts, and it is mediated by a small segment of roughly a dozen residues that lie within a natively unstructured sub-domain of RNase E. Here, we present the crystal structure of enolase in complex with its recognition site from RNase E at 1.6A resolution. A single molecule of the RNase E peptide binds asymmetrically in a conserved cleft at the interface of the enolase dimer. The recognition site is well conserved in RNase E homologues in a subfamily of the gamma-proteobacteria, including enzymes from pathogens such as Yersinia pestis, Vibrio cholera and Salmonella sp. We suggest that enolase is recruited into putative RNA degradosome machinery in these bacilli, where it plays common regulatory functions.

PubMed: 16516921
DOI: 10.1016/j.jmb.2006.02.012

実験手法

X-RAY DIFFRACTION (1.6 Å)