4FYG
Structural basis for substrate recognition by a novel Legionella phosphoinositide phosphatase
Summary for 4FYG
Entry DOI | 10.2210/pdb4fyg/pdb |
Related | 4FYE 4FYF |
Descriptor | SidF, inhibitor of growth family, member 3, (2R)-3-{[(S)-hydroxy{[(1S,2R,3R,4S,5S,6S)-2,3,6-trihydroxy-4,5-bis(phosphonooxy)cyclohexyl]oxy}phosphoryl]oxy}propane-1,2-diyl dibutanoate (3 entities in total) |
Functional Keywords | mixed alpha-beta, phosphoinositide phosphatase, phosphoinositides, membrane, hydrolase |
Biological source | Legionella pneumophila subsp. pneumophila |
Total number of polymer chains | 1 |
Total formula weight | 86825.71 |
Authors | |
Primary citation | 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 Cited by 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: 22872863DOI: 10.1073/pnas.1207903109 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.822 Å) |
Structure validation
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