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6vvc

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Current revision (14:39, 6 March 2024) (edit) (undo)
 
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<StructureSection load='6vvc' size='340' side='right'caption='[[6vvc]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='6vvc' size='340' side='right'caption='[[6vvc]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6vvc]] is a 1 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=6VVC OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6VVC FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6vvc]] is a 1 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=6VVC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VVC FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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]] 2.1&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">C3927_13135, DI056_05180, DI105_03620 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=446 ATCC 33152])</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=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6vvc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vvc OCA], [http://pdbe.org/6vvc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6vvc RCSB], [http://www.ebi.ac.uk/pdbsum/6vvc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6vvc ProSAT]</span></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=6vvc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vvc OCA], [https://pdbe.org/6vvc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vvc RCSB], [https://www.ebi.ac.uk/pdbsum/6vvc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vvc 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/Q5ZSB6_LEGPH Q5ZSB6_LEGPH]
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The transfer of a phosphate from ATP to a protein substrate, a modification known as protein phosphorylation, is catalyzed by protein kinases. Protein kinases play a crucial role in virtually every cellular activity. Recent studies of atypical protein kinases have highlighted the structural similarity of the kinase superfamily despite notable differences in primary amino acid sequence. Here, using a bioinformatics screen, we searched for putative protein kinases in the intracellular bacterial pathogen Legionella pneumophila and identified the type 4 secretion system (T4SS) effector Lpg2603 as a remote member of the protein kinase superfamily. Employing an array of biochemical and structural biology approaches, including in vitro kinase assays and isothermal calorimetry, we show that Lpg2603 is an active protein kinase with several atypical structural features. Importantly, we found that the eukaryote-specific host signaling molecule inositol hexakisphosphate (IP6) is required for Lpg2603 kinase activity. Crystal structures of Lpg2603 in the apo-form and when bound to IP6 revealed an active-site rearrangement that allows for ATP binding and catalysis. Our results on the structure and activity of Lpg2603 reveal a unique mode of regulation of a protein kinase, provide the first example of a bacterial kinase that requires IP6 for its activation, and may aid future work on the function of this effector during Legionella pathogenesis.
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A Legionella effector kinase is activated by host inositol hexakisphosphate.,Sreelatha A, Nolan C, Park BC, Pawlowski K, Tomchick DR, Tagliabracci VS J Biol Chem. 2020 Mar 30. pii: RA120.013067. doi: 10.1074/jbc.RA120.013067. PMID:32229585<ref>PMID:32229585</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 6vvc" 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: Atcc 33152]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Park, B C]]
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[[Category: Legionella pneumophila]]
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[[Category: Tagliabracci, V S]]
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[[Category: Park BC]]
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[[Category: Tomchick, D R]]
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[[Category: Tagliabracci VS]]
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[[Category: Kinase]]
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[[Category: Tomchick DR]]
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[[Category: Phosphorylation]]
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[[Category: Transferase]]
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Current revision

Legionella pneumophila Lpg2603 kinase

PDB ID 6vvc

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