4fyg

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==Structural basis for substrate recognition by a novel Legionella phosphoinositide phosphatase==
==Structural basis for substrate recognition by a novel Legionella phosphoinositide phosphatase==
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<StructureSection load='4fyg' size='340' side='right' caption='[[4fyg]], [[Resolution|resolution]] 2.82&Aring;' scene=''>
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<StructureSection load='4fyg' size='340' side='right'caption='[[4fyg]], [[Resolution|resolution]] 2.82&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4fyg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Legionella_pneumophila_subsp._pneumophila Legionella pneumophila subsp. pneumophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FYG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FYG FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4fyg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Legionella_pneumophila_subsp._pneumophila_str._Philadelphia_1 Legionella pneumophila subsp. pneumophila str. Philadelphia 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FYG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FYG FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3PT:(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'>3PT</scene><br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.822&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4fye|4fye]], [[4fyf|4fyf]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3PT:(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'>3PT</scene></td></tr>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lpg2584, sidF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=91891 Legionella pneumophila subsp. pneumophila])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4fyg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fyg OCA], [https://pdbe.org/4fyg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fyg RCSB], [https://www.ebi.ac.uk/pdbsum/4fyg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fyg ProSAT]</span></td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphatidylinositol-3,4,5-trisphosphate_3-phosphatase Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.67 3.1.3.67] </span></td></tr>
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</table>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4fyg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fyg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fyg RCSB], [http://www.ebi.ac.uk/pdbsum/4fyg PDBsum]</span></td></tr>
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== Function ==
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<table>
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[https://www.uniprot.org/uniprot/Q5ZSD5_LEGPH Q5ZSD5_LEGPH]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Structural basis for substrate recognition by a unique Legionella phosphoinositide phosphatase.,Hsu F, Zhu W, Brennan L, Tao L, Luo ZQ, Mao Y Proc Natl Acad Sci U S A. 2012 Aug 7. PMID:22872863<ref>PMID:22872863</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Legionella pneumophila subsp. pneumophila]]
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[[Category: Large Structures]]
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[[Category: Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase]]
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[[Category: Legionella pneumophila subsp. pneumophila str. Philadelphia 1]]
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[[Category: Brennan, L.]]
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[[Category: Brennan L]]
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[[Category: Hsu, F S.]]
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[[Category: Hsu FS]]
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[[Category: Luo, Z Q.]]
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[[Category: Luo ZQ]]
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[[Category: Mao, Y.]]
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[[Category: Mao Y]]
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[[Category: Tao, L.]]
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[[Category: Tao L]]
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[[Category: Zhu, W.]]
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[[Category: Zhu W]]
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[[Category: Hydrolase]]
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[[Category: Membrane]]
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[[Category: Mixed alpha-beta]]
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[[Category: Phosphoinositide phosphatase]]
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[[Category: Phosphoinositide]]
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Current revision

Structural basis for substrate recognition by a novel Legionella phosphoinositide phosphatase

PDB ID 4fyg

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