7OL1

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

Summary for 7OL1

Entry DOI	10.2210/pdb7ol1/pdb
Descriptor	L-threonine 3-dehydrogenase (2 entities in total)
Functional Keywords	dehydrogenase, apoenzyme., oxidoreductase
Biological source	Clostridioides difficile (Peptoclostridium difficile)
Total number of polymer chains	2
Total formula weight	76416.70
Authors	Guo, J.,Cooper, J.B. (deposition date: 2021-05-18, release date: 2021-06-16, Last modification date: 2024-01-31)
Primary citation	Adjogatse, E.,Bennett, J.,Guo, J.,Erskine, P.T.,Wood, S.P.,Wren, B.W.,Cooper, J.B. The X-ray structure of L-threonine dehydrogenase from the common hospital pathogen Clostridium difficile. Acta Crystallogr.,Sect.F, 77:269-274, 2021 Cited by PubMed 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. PubMed: 34341193 DOI: 10.1107/S2053230X21007135 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.6 Å)

Structure validation