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7vkb

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'''Unreleased structure'''
 
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The entry 7vkb is ON HOLD
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==Crystal structure of the a bacterial kinase complex==
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<StructureSection load='7vkb' size='340' side='right'caption='[[7vkb]], [[Resolution|resolution]] 1.82&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[7vkb]] is a 2 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=7VKB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7VKB 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=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=7vkb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7vkb OCA], [https://pdbe.org/7vkb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7vkb RCSB], [https://www.ebi.ac.uk/pdbsum/7vkb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7vkb ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[https://www.uniprot.org/uniprot/Q5ZSZ6_LEGPH Q5ZSZ6_LEGPH]]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Toxin-antitoxin (TA) systems are ubiquitous genetic modules in bacteria and archaea. Here, we perform structural and biochemical characterization of the Legionella pneumophila effector Lpg2370, demonstrating that it is a Ser/Thr kinase. Together with two upstream genes, lpg2370 constitutes the tripartite HipBST TA. Notably, the toxin Lpg2370 (HipTLp) and the antitoxin Lpg2369 (HipSLp) correspond to the C-terminus and N-terminus of HipA from HipBA TA, respectively. By determining crystal structures of autophosphorylated HipTLp, its complex with AMP-PNP, and the structure of HipTLp-HipSLp complex, we identify residues in HipTLp critical for ATP binding and those contributing to its interactions with HipSLp. Structural analysis reveals that HipSLp binding induces a loop-to-helix shift in the P-loop of HipTLp, leading to the blockage of ATP binding and inhibition of the kinase activity. These findings establish the L. pneumophila effector Lpg2370 as the HipBST TA toxin and elucidate the molecular basis for HipT neutralization in HipBST TA.
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Authors: Zhen, X.
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Molecular mechanism of toxin neutralization in the HipBST toxin-antitoxin system of Legionella pneumophila.,Zhen X, Wu Y, Ge J, Fu J, Ye L, Lin N, Huang Z, Liu Z, Luo ZQ, Qiu J, Ouyang S Nat Commun. 2022 Jul 26;13(1):4333. doi: 10.1038/s41467-022-32049-x. PMID:35882877<ref>PMID:35882877</ref>
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Description: Crystal struture of the a bacterial kinase complex
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Zhen, X]]
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<div class="pdbe-citations 7vkb" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Legionella pneumophila subsp. pneumophila str. Philadelphia 1]]
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[[Category: Ouyang SY]]
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[[Category: Zhen X]]

Current revision

Crystal structure of the a bacterial kinase complex

PDB ID 7vkb

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