5n6x

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==Crystal structure of the Legionella effector WipA==
==Crystal structure of the Legionella effector WipA==
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<StructureSection load='5n6x' size='340' side='right' caption='[[5n6x]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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<StructureSection load='5n6x' size='340' side='right'caption='[[5n6x]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5n6x]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N6X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5N6X FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5n6x]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Legionella_pneumophila Legionella pneumophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N6X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5N6X FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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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]] 1.75&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5n6x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n6x OCA], [http://pdbe.org/5n6x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5n6x RCSB], [http://www.ebi.ac.uk/pdbsum/5n6x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5n6x ProSAT]</span></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=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=5n6x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n6x OCA], [https://pdbe.org/5n6x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5n6x RCSB], [https://www.ebi.ac.uk/pdbsum/5n6x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5n6x ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q5GA16_LEGPN Q5GA16_LEGPN]
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Legionnaires disease is a severe form of pneumonia caused by the bacterium Legionella pneumophila. L. pneumophila pathogenicity relies on secretion of more than 300 effector proteins by a type IVb secretion system. Among these Legionella effectors, WipA has been primarily studied because of its dependence on a chaperone complex, IcmSW, for translocation through the secretion system, but its role in pathogenicity has remained unknown. In this study, we present the crystal structure of a large fragment of WipA, WipA435. Surprisingly, this structure revealed a serine/threonine phosphatase fold that unexpectedly targets tyrosine-phosphorylated peptides. The structure also revealed a sequence insertion that folds into an alpha-helical hairpin, the tip of which adopts a canonical coiled-coil structure. The purified protein was a dimer, whose dimer interface involves interactions between the coiled-coil of one WipA molecule and the phosphatase domain of another. Given the ubiquity of protein-protein interaction mediated by interactions between coiled-coils, we hypothesize that WipA can thereby transition from a homo-dimeric state to a hetero-dimeric state in which the coiled-coil region of WipA is engaged in a protein-protein interaction with a tyrosine-phosphorylated host target. In conclusion, these findings help advance our understanding of the molecular mechanisms of an effector involved in Legionella virulence and may inform approaches to elucidate the function of other effectors.
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Structure of the WipA protein reveals a novel tyrosine protein phosphatase effector from Legionella pneumophila.,Pinotsis N, Waksman G J Biol Chem. 2017 Apr 7. pii: jbc.M117.781948. doi: 10.1074/jbc.M117.781948. PMID:28389563<ref>PMID:28389563</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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<div class="pdbe-citations 5n6x" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Pinotsis, N]]
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[[Category: Large Structures]]
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[[Category: Waksman, G]]
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[[Category: Legionella pneumophila]]
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[[Category: Coiled-coil]]
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[[Category: Pinotsis N]]
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[[Category: Hydrolase]]
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[[Category: Waksman G]]
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[[Category: Legionella effector]]
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[[Category: Phosphoesterase fold]]
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[[Category: Tyrosine phosphatase]]
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Current revision

Crystal structure of the Legionella effector WipA

PDB ID 5n6x

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