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Sci Rep. 2019 Mar 13;9(1):4392. doi: 10.1038/s41598-019-40558-x.

Crystal structures of thiamine monophosphate kinase from Acinetobacter baumannii in complex with substrates and products.

Author information

1
UCB/Beryllium Discovery, 98110, 7869 NE Day Road West, Bainbridge Island, WA, USA.
2
Seattle Structural Genomics Center for Infectious Disease, Seattle, WA, USA.
3
UCB/Beryllium Discovery, 98110, 7869 NE Day Road West, Bainbridge Island, WA, USA. jan.abendroth@ucb.com.
4
Seattle Structural Genomics Center for Infectious Disease, Seattle, WA, USA. jan.abendroth@ucb.com.

Abstract

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.

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