3NKU

Crystal structure of the N-terminal domain of DrrA/SidM from Legionella pneumophila

3NKU の概要

• エントリーDOI: 10.2210/pdb3nku/pdb
• 分子名称: DrrA, DI(HYDROXYETHYL)ETHER, TRIETHYLENE GLYCOL, ... (4 entities in total)
• 機能のキーワード: posttranslational modification, ampylation, adenylylation, rab1b, rab1, drra, sidm, vesicular transport, protein transport
• 由来する生物種: Legionella pneumophila subsp. pneumophila
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 49359.00

構造登録者

Mueller, M.P.,Peters, H.,Blankenfeldt, W.,Goody, R.S.,Itzen, A. (登録日: 2010-06-21, 公開日: 2010-08-04, 最終更新日: 2024-11-20)

主引用文献

Muller, M.P.,Peters, H.,Blumer, J.,Blankenfeldt, W.,Goody, R.S.,Itzen, A.
The Legionella effector protein DrrA AMPylates the membrane traffic regulator Rab1b.
Science, 329:946-949, 2010

PubMed Abstract: In the course of Legionnaires' disease, the bacterium Legionella pneumophila affects the intracellular vesicular trafficking of infected eukaryotic cells by recruiting the small guanosine triphosphatase (GTPase) Rab1 to the cytosolic face of the Legionella-containing vacuole. In order to accomplish this, the Legionella protein DrrA contains a specific guanine nucleotide exchange activity for Rab1 activation that exchanges guanosine triphosphate (GTP) for guanosine diphosphate on Rab1. We found that the amino-terminal domain of DrrA possesses adenosine monophosphorylation (AMPylation) activity toward the switch II region of Rab1b, leading to posttranslational covalent modification of tyrosine 77. AMPylation of switch II by DrrA restricts the access of GTPase activating proteins, thereby rendering Rab1b constitutively active.

PubMed: 20651120
DOI: 10.1126/science.1192276

実験手法

X-RAY DIFFRACTION (2.1 Å)