4FYF

Structural basis for substrate recognition by a novel Legionella phosphoinositide phosphatase

4FYF の概要

• エントリーDOI: 10.2210/pdb4fyf/pdb
• 関連するPDBエントリー: 4FYE
• 分子名称: SidF, inhibitor of growth family, member 3, PHOSPHATE ION, MERCURY (II) ION, ... (4 entities in total)
• 機能のキーワード: mixed alpha-beta, phosphoinositide phosphatase, phosphoinositides, membrane, hydrolase
• 由来する生物種: Legionella pneumophila subsp. pneumophila
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 86888.10

構造登録者

Hsu, F.S.,Zhu, W.,Brennan, L.,Tao, L.,Luo, Z.Q.,Mao, Y. (登録日: 2012-07-04, 公開日: 2012-08-22, 最終更新日: 2024-04-03)

主引用文献

Hsu, F.,Zhu, W.,Brennan, L.,Tao, L.,Luo, Z.Q.,Mao, Y.
Structural basis for substrate recognition by a unique Legionella phosphoinositide phosphatase.
Proc.Natl.Acad.Sci.USA, 109:13567-13572, 2012

PubMed Abstract: Legionella pneumophila is an opportunistic intracellular pathogen that causes sporadic and epidemic cases of Legionnaires' disease. Emerging data suggest that Legionella infection involves the subversion of host phosphoinositide (PI) metabolism. However, how this bacterium actively manipulates PI lipids to benefit its infection is still an enigma. Here, we report that the L. pneumophila virulence factor SidF is a phosphatidylinositol polyphosphate 3-phosphatase that specifically hydrolyzes the D3 phosphate of PI(3,4)P(2) and PI(3,4,5)P(3). This activity is necessary for anchoring of PI(4)P-binding effectors to bacterial phagosomes. Crystal structures of SidF and its complex with its substrate PI(3,4)P(2) reveal striking conformational rearrangement of residues at the catalytic site to form a cationic pocket that specifically accommodates the D4 phosphate group of the substrate. Thus, our findings unveil a unique Legionella PI phosphatase essential for the establishment of lipid identity of bacterial phagosomes.

PubMed: 22872863
DOI: 10.1073/pnas.1207903109

実験手法

X-RAY DIFFRACTION (2.424 Å)