Journal
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
Volume 86, Issue 12, Pages 1306-1312Publisher
WILEY
DOI: 10.1002/prot.25606
Keywords
4-epimerase; EPZ; Methanobrevibacter; Pseudomurein; UDP-GlcNAc 4-epimerase; UDP-N-acetylglucosamine; UDP-N-acetylmuramic acid; WbpP
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Funding
- Pastoral Greenhouse Gas Research Consortium
- Royal Society of New Zealand [AGR1301]
- Marsden Fund
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The crystal structure of UDP-N-acetylglucosamine 4-epimerase (UDP-GlcNAc 4-epimerase; WbpP; EC 5.1.3.7), from the archaeal methanogen Methanobrevibacter ruminantium strain M1, was determined to a resolution of 1.65 angstrom. The structure, with a single monomer in the crystallographic asymmetric unit, contained a conserved N-terminal Rossmann-fold for nucleotide binding and an active site positioned in the C-terminus. UDP-GlcNAc 4-epimerase is a member of the short-chain dehydrogenases/reductases superfamily, sharing sequence motifs and structural elements characteristic of this family of oxidoreductases and bacterial 4-epimerases. The protein was co-crystallized with coenzyme NADH and UDP-N-acetylmuramic acid, the latter an unintended inclusion and well known product of the bacterial enzyme MurB and a critical intermediate for bacterial cell wall synthesis. This is a non-native UDP sugar amongst archaea and was most likely incorporated from the E. coli expression host during purification of the recombinant enzyme.
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