3JSZ

Legionella pneumophila glucosyltransferase Lgt1 N293A with UDP-Glc

3JSZ の概要

• エントリーDOI: 10.2210/pdb3jsz/pdb
• 関連するPDBエントリー: 3JT1
• 分子名称: Putative uncharacterized protein, URIDINE-5'-DIPHOSPHATE-GLUCOSE, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: glucosyltransferase, legionnaire's disease, legionella pneumophila, transferase
• 由来する生物種: Legionella pneumophila
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 60691.03

構造登録者

Lu, W.,Du, J.,Belyi, Y.,Stahl, M.,Zivilikidis, T.,Gerhardt, S.,Aktories, K.,Einsle, O. (登録日: 2009-09-11, 公開日: 2010-02-02, 最終更新日: 2024-11-13)

主引用文献

Lu, W.,Du, J.,Stahl, M.,Tzivelekidis, T.,Belyi, Y.,Gerhardt, S.,Aktories, K.,Einsle, O.
Structural Basis of the Action of Glucosyltransferase Lgt1 from Legionella pneumophila.
J.Mol.Biol., 2009

PubMed Abstract: The glucosyltransferase Lgt1 is one of three glucosylating toxins of Legionella pneumophila, the causative agent of Legionnaires disease. It acts through specific glucosylation of a serine residue (S53) in the eukaryotic elongation factor 1A and belongs to type A glycosyltransferases. High-resolution crystal structures of Lgt1 show an elongated shape of the protein, with the binding site for uridine disphosphate glucose at the bottom of a deep cleft. Lgt1 shows only a low sequence identity with other type A glycosyltransferases, and structural conservation is limited to a central folding core that is usually observed within this family of proteins. Domains and protrusions added to the core motif represent determinants for the specific recognition and binding of the target. Manual docking experiments based on the crystal structures of toxin and target protein suggest an obvious mode of binding to the target that allows for efficient transfer of a glucose moiety.

PubMed: 19941871
DOI: 10.1016/j.jmb.2009.11.044

実験手法

X-RAY DIFFRACTION (1.7 Å)