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The X-ray structure of L -threonine dehydrogenase from the common hospital pathogen Clostridium difficile

DOI: 10.1107/S2053230X21007135 DOI Help

Authors: Eyram Adjogatse (University College London) , Josh Bennett (University College London) , Jingxu Guo (University College London; University of Cambridge School of Clinical Medicine) , Peter T. Erskine (University College London; Birkbeck, University of London) , Steve P. Wood (University College London; University of Portsmouth) , Brendan W. Wren (London School of Hygiene and Tropical Medicine) , Jonathan B. Cooper (University College London; Birkbeck, University of London)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology Communications , VOL 77 , PAGES 269 - 274

State: Published (Approved)
Published: August 2021
Diamond Proposal Number(s): 7131

Abstract: In many prokaryotes, the first step of threonine metabolism is catalysed by the enzyme threonine dehydrogenase (TDH), which uses NAD+ to oxidize its substrate to 2-amino-3-ketobutyrate. The absence of a functional TDH gene in humans suggests that inhibitors of this enzyme may have therapeutic potential against pathogens which are reliant on this enzyme. Here, TDH from Clostridium difficile has been cloned and overexpressed, and the X-ray structure of the apoenzyme form has been determined at 2.6 Å resolution.

Journal Keywords: threonine dehydrogenase; Clostridium difficile; protein crystallography; molecular replacement; refinement

Diamond Keywords: Bacteria; Enzymes

Subject Areas: Biology and Bio-materials, Chemistry, Medicine

Instruments: I04-1-Macromolecular Crystallography (fixed wavelength)

Added On: 03/08/2021 08:27

Discipline Tags:

Pathogens Infectious Diseases Health & Wellbeing Biochemistry Catalysis Chemistry Structural biology Drug Discovery Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)