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

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.

journal_name

Sci Rep

journal_title

Scientific reports

authors

Sullivan AH,Dranow DM,Horanyi PS,Lorimer DD,Edwards TE,Abendroth J

doi

10.1038/s41598-019-40558-x

subject

Has Abstract

pub_date

2019-03-13 00:00:00

pages

4392

issue

1

issn

2045-2322

pii

10.1038/s41598-019-40558-x

journal_volume

9

pub_type

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