6YX5

Structure of DrrA from Legionella pneumophilia in complex with human Rab8a

6YX5 の概要

• エントリーDOI: 10.2210/pdb6yx5/pdb
• 分子名称: Ras-related protein Rab-8A, Multifunctional virulence effector protein DrrA, MAGNESIUM ION, ... (8 entities in total)
• 機能のキーワード: vesicular trafficking virulence factor, cell invasion
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 60798.89

構造登録者

Schneider, S.,Du, J.,von Wrisberg, M.K.,Lang, K.,Itzen, A. (登録日: 2020-04-30, 公開日: 2020-12-23, 最終更新日: 2024-11-20)

主引用文献

Du, J.,Wrisberg, M.V.,Gulen, B.,Stahl, M.,Pett, C.,Hedberg, C.,Lang, K.,Schneider, S.,Itzen, A.
Rab1-AMPylation by Legionella DrrA is allosterically activated by Rab1.
Nat Commun, 12:460-460, 2021

PubMed Abstract: Legionella pneumophila infects eukaryotic cells by forming a replicative organelle - the Legionella containing vacuole. During this process, the bacterial protein DrrA/SidM is secreted and manipulates the activity and post-translational modification (PTM) states of the vesicular trafficking regulator Rab1. As a result, Rab1 is modified with an adenosine monophosphate (AMP), and this process is referred to as AMPylation. Here, we use a chemical approach to stabilise low-affinity Rab:DrrA complexes in a site-specific manner to gain insight into the molecular basis of the interaction between the Rab protein and the AMPylation domain of DrrA. The crystal structure of the Rab:DrrA complex reveals a previously unknown non-conventional Rab-binding site (NC-RBS). Biochemical characterisation demonstrates allosteric stimulation of the AMPylation activity of DrrA via Rab binding to the NC-RBS. We speculate that allosteric control of DrrA could in principle prevent random and potentially cytotoxic AMPylation in the host, thereby perhaps ensuring efficient infection by Legionella.

PubMed: 33469029
DOI: 10.1038/s41467-020-20702-2

実験手法

X-RAY DIFFRACTION (2.14 Å)