3GND

Crystal Structure of E. coli LsrF in complex with Ribulose-5-phosphate

3GND の概要

• エントリーDOI: 10.2210/pdb3gnd/pdb
• 関連するPDBエントリー: 3GKF 3GLC
• 分子名称: Aldolase lsrF, RIBULOSE-5-PHOSPHATE (3 entities in total)
• 機能のキーワード: tim barrel, lyase, schiff base
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm : P76143
• タンパク質・核酸の鎖数: 20
• 化学式量合計: 651045.10

構造登録者

Miller, S.T.,Diaz, Z.C. (登録日: 2009-03-17, 公開日: 2009-09-08, 最終更新日: 2023-09-06)

主引用文献

Diaz, Z.,Xavier, K.B.,Miller, S.T.
The crystal structure of the Escherichia coli autoinducer-2 processing protein LsrF.
Plos One, 4:e6820-e6820, 2009

PubMed Abstract: Many bacteria produce and respond to the quorum sensing signal autoinducer-2 (AI-2). Escherichia coli and Salmonella typhimurium are among the species with the lsr operon, an operon containing AI-2 transport and processing genes that are up regulated in response to AI-2. One of the Lsr proteins, LsrF, has been implicated in processing the phosphorylated form of AI-2. Here, we present the structure of LsrF, unliganded and in complex with two phospho-AI-2 analogues, ribose-5-phosphate and ribulose-5-phosphate. The crystal structure shows that LsrF is a decamer of (alphabeta)(8)-barrels that exhibit a previously unseen N-terminal domain swap and have high structural homology with aldolases that process phosphorylated sugars. Ligand binding sites and key catalytic residues are structurally conserved, strongly implicating LsrF as a class I aldolase.

PubMed: 19714241
DOI: 10.1371/journal.pone.0006820

実験手法

X-RAY DIFFRACTION (2.9 Å)