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    Thiamine monophosphate kinase (ThiL) catalyzes the last step of thiamine pyrophosphate (TPP) synthesis, the ATP-dependent phosphorylation of thiamine monophosphate (TMP) to thiamine pyrophosphate. We solved the structure of ThiL from the human pathogen A. baumanii in complex with a pair of substrates TMP and a non-hydrolyzable adenosine triphosphate analog, and in complex with a pair of products TPP and adenosine diphosphate. High resolution of the data and anomalous diffraction allows for a detailed description of the binding mode of substrates and products, and their metal environment. The structures further support a previously proposed in-line attack reaction mechanism and show a distinct variability of metal content of the active site.


    Amy H Sullivan, David M Dranow, Peter S Horanyi, Donald D Lorimer, Thomas E Edwards, Jan Abendroth. Crystal structures of thiamine monophosphate kinase from Acinetobacter baumannii in complex with substrates and products. Scientific reports. 2019 Mar 13;9(1):4392

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    PMID: 30867460

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