ATP and autophosphorylation driven conformational changes of HipA kinase revealed by ion mobility and crosslinking mass spectrometry

ATP and autophosphorylation driven conformational changes of HipA kinase revealed by ion mobility and crosslinking mass spectrometry
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离子淌度和交联质谱揭示 ATP 和自磷酸化驱动的 HipA 激酶构象变化

DOI:
10.1007/s00216-016-9709-3
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发表时间:
2016-06
影响因子:
4.3
通讯作者:
Devreese Bart
Devreese Bart
中科院分区:
化学2区
文献类型:
--
作者:
Wen Yurong;Sobott Frank;Devreese Bart

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Toxin-antitoxin systems are genetic modules involved in a broad range of bacterial cellular processes including persistence, multidrug resistance and tolerance, biofilm formation, and pathogenesis. In type II toxin-antitoxin systems, both the toxin and antitoxin are proteins. In the prototypicEscherichia coliHipA-HipB module, the antitoxin HipB forms a complex with the protein kinase HipA and sequesters it in the nucleoid. HipA is then no longer able to phosphorylate glutamyl-tRNA-synthetase and this prevents the initiation of the forthcoming stringent response. Here we investigated the assembly of theShewanella oneidensisMR-1 HipA-HipB complex using native electrospray ion mobility-mass spectrometry and chemical crosslinking combined with mass spectrometry. We revealed that the HipA autophosphorylation was accompanied by a large conformational change, and confirmed structural evidence thatS. oneidensisMR-1 HipA-HipB assembly was distinct from the prototypicE. coliHipA-HipB complex.Graphical abstractIon mobility mass spectrometry shows a two phase transition from unstructured HipA to a compact folded phosphorylated protein
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