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| | <StructureSection load='5uf5' size='340' side='right'caption='[[5uf5]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='5uf5' size='340' side='right'caption='[[5uf5]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5uf5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_33152 Atcc 33152]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UF5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UF5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5uf5]] 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=5UF5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UF5 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ufk|5ufk]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lpg_0968 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=446 ATCC 33152])</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5uf5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uf5 OCA], [https://pdbe.org/5uf5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5uf5 RCSB], [https://www.ebi.ac.uk/pdbsum/5uf5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5uf5 ProSAT]</span></td></tr> |
| - | <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=5uf5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uf5 OCA], [http://pdbe.org/5uf5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5uf5 RCSB], [http://www.ebi.ac.uk/pdbsum/5uf5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5uf5 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/Q5ZWW6_LEGPH Q5ZWW6_LEGPH] |
| - | Intracellular pathogenic bacteria evade the immune response by replicating within host cells. Legionella pneumophila, the causative agent of Legionnaires' Disease, makes use of numerous effector proteins to construct a niche supportive of its replication within phagocytic cells. The L. pneumophila effector SidK was identified in a screen for proteins that reduce the activity of the proton pumping vacuolar-type ATPases (V-ATPases) when expressed in the yeast Saccharomyces cerevisae. SidK is secreted by L. pneumophila in the early stages of infection and by binding to and inhibiting the V-ATPase, SidK reduces phagosomal acidification and promotes survival of the bacterium inside macrophages. We determined crystal structures of the N-terminal region of SidK at 2.3 A resolution and used single particle electron cryomicroscopy (cryo-EM) to determine structures of V-ATPase:SidK complexes at ~6.8 A resolution. SidK is a flexible and elongated protein composed of an alpha-helical region that interacts with subunit A of the V-ATPase and a second region of unknown function that is flexibly-tethered to the first. SidK binds V-ATPase strongly by interacting via two alpha-helical bundles at its N terminus with subunit A. In vitro activity assays show that SidK does not inhibit the V-ATPase completely, but reduces its activity by ~40%, consistent with the partial V-ATPase deficiency phenotype its expression causes in yeast. The cryo-EM analysis shows that SidK reduces the flexibility of the A-subunit that is in the 'open' conformation. Fluorescence experiments indicate that SidK binding decreases the affinity of V-ATPase for a fluorescent analogue of ATP. Together, these results reveal the structural basis for the fine-tuning of V-ATPase activity by SidK.
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| - | | + | |
| - | Molecular basis for the binding and modulation of V-ATPase by a bacterial effector protein.,Zhao J, Beyrakhova K, Liu Y, Alvarez CP, Bueler SA, Xu L, Xu C, Boniecki MT, Kanelis V, Luo ZQ, Cygler M, Rubinstein JL PLoS Pathog. 2017 Jun 1;13(6):e1006394. doi: 10.1371/journal.ppat.1006394., eCollection 2017 Jun. PMID:28570695<ref>PMID:28570695</ref>
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| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 5uf5" style="background-color:#fffaf0;"></div>
| + | |
| - | == References ==
| + | |
| - | <references/>
| + | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 33152]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Beyrakhova, K]] | + | [[Category: Legionella pneumophila]] |
| - | [[Category: Boniecki, M T]] | + | [[Category: Beyrakhova K]] |
| - | [[Category: Cygler, M]] | + | [[Category: Boniecki MT]] |
| - | [[Category: Xu, C]] | + | [[Category: Cygler M]] |
| - | [[Category: All-alpha-helical]]
| + | [[Category: Xu C]] |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: Translocated effector]]
| + | |
| - | [[Category: V-atpase binding]]
| + | |
