7vkb
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<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> | <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> | ||
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.82Å</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> | ||
<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> | <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> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/Q5ZSZ6_LEGPH Q5ZSZ6_LEGPH] | |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| - | 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 ( | + | 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 (HipT(Lp)) and the antitoxin Lpg2369 (HipS(Lp)) correspond to the C-terminus and N-terminus of HipA from HipBA TA, respectively. By determining crystal structures of autophosphorylated HipT(Lp), its complex with AMP-PNP, and the structure of HipT(Lp)-HipS(Lp) complex, we identify residues in HipT(Lp) critical for ATP binding and those contributing to its interactions with HipS(Lp). Structural analysis reveals that HipS(Lp) binding induces a loop-to-helix shift in the P-loop of HipT(Lp), 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. |
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> | 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> | ||
Current revision
Crystal structure of the a bacterial kinase complex
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