4XI1

Crystal structure of U-box 2 of LubX / LegU2 / Lpp2887 from Legionella pneumophila str. Paris, wild-type

「4WZ1」から置き換えられました

4XI1 の概要

• エントリーDOI: 10.2210/pdb4xi1/pdb
• 関連するPDBエントリー: 4WZ0 4WZ1 4WZ2 4WZ3
• 分子名称: E3 ubiquitin-protein ligase LubX, CHLORIDE ION, HEXANE-1,6-DIOL, ... (5 entities in total)
• 機能のキーワード: alpha/beta protein, effector, structural genomics, psi-biology, midwest center for structural genomics, mcsg, ligase
• 由来する生物種: Legionella pneumophila (strain Paris)
• 細胞内の位置: Secreted : Q5X159
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 36077.35

構造登録者

Stogios, P.J.,Quaile, T.,Skarina, T.,Cuff, M.,Di Leo, R.,Yim, V.,Savchenko, A.,Joachimiak, A.,Midwest Center for Structural Genomics (MCSG) (登録日: 2015-01-06, 公開日: 2015-01-21, 最終更新日: 2023-09-27)

主引用文献

Quaile, A.T.,Urbanus, M.L.,Stogios, P.J.,Nocek, B.,Skarina, T.,Ensminger, A.W.,Savchenko, A.
Molecular Characterization of LubX: Functional Divergence of the U-Box Fold by Legionella pneumophila.
Structure, 23:1459-1469, 2015

PubMed Abstract: LubX is part of the large arsenal of effectors in Legionella pneumophila that are translocated into the host cytosol during infection. Despite such unique features as the presence of two U-box motifs and its targeting of another effector SidH, the molecular basis of LubX activity remains poorly understood. Here we show that the N terminus of LubX is able to activate an extended number of ubiquitin-conjugating (E2) enzymes including UBE2W, UBEL6, and all tested members of UBE2D and UBE2E families. Crystal structures of LubX alone and in complex with UBE2D2 revealed drastic molecular diversification between the two U-box domains, with only the N-terminal U-box retaining E2 recognition features typical for its eukaryotic counterparts. Extensive mutagenesis followed by functional screening in a yeast model system captured functionally important LubX residues including Arg121, critical for interactions with SidH. Combined, these data provide a new molecular insight into the function of this unique pathogenic factor.

PubMed: 26146184
DOI: 10.1016/j.str.2015.05.020

実験手法

X-RAY DIFFRACTION (2.983 Å)