3H8A

Crystal structure of E. coli enolase bound to its cognate RNase E recognition domain

3H8A の概要

• エントリーDOI: 10.2210/pdb3h8a/pdb
• 分子名称: Enolase, RNase E, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: glycolytic enzyme, protein-protein interaction, lyase, metal-binding, lyase-protein binding complex, lyase/protein binding
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Cytoplasm, cytoskeleton: P0A6P9
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 188971.03

構造登録者

Nurmohamed, S.,Luisi, B.F. (登録日: 2009-04-29, 公開日: 2010-04-14, 最終更新日: 2023-09-06)

主引用文献

Nurmohamed, S.,McKay, A.R.,Robinson, C.V.,Luisi, B.F.
Molecular recognition between Escherichia coli enolase and ribonuclease E.
Acta Crystallogr.,Sect.D, 66:1036-1040, 2010

PubMed Abstract: In Escherichia coli and many other bacterial species, the glycolytic enzyme enolase is a component of the multi-enzyme RNA degradosome, an assembly that is involved in RNA processing and degradation. Enolase is recruited into the degradosome through interactions with a small recognition motif located within the degradosome-scaffolding domain of RNase E. Here, the crystal structure of enolase bound to its cognate site from RNase E (residues 823-850) at 1.9 A resolution is presented. The structure suggests that enolase may help to organize an adjacent conserved RNA-binding motif in RNase E.

PubMed: 20823555
DOI: 10.1107/S0907444910030015

実験手法

X-RAY DIFFRACTION (1.9 Å)