Insights into structure and activity of a UDP-GlcNAc 2-epimerase involved in secondary cell wall polymer biosynthesis in Paenibacillus alvei
The unliganded crystal structure of <i>P. alvei</i> MnaA reveals an open conformation characterized by an accessible cleft between the N- and C-terminal domains. Despite the conservation of residues involved in binding the allosteric activator UDP-GlcNAc, the enzyme is not strictly regulated by the substrate. Unlike <i>S. aureus</i> MnaA, the activity of <i>P. alvei</i> MnaA remains unaffected by tunicamycin.
Authors
- Christina Schäffer (ORCID: https://orcid.org/0000-0003-1613-7258)
- Max S G Legg (ORCID: https://orcid.org/0000-0002-9065-7019)
- Stephen V. Evans (ORCID: https://orcid.org/0000-0002-0366-4027)
- Chris Oostenbrink (ORCID: https://orcid.org/0000-0002-4232-2556)
- Fiona F. Hager‐Mair (ORCID: https://orcid.org/0000-0001-9586-5127)
- Cordula Stefanović
- Nick Mateyko
- Tea Kuvek
- Jakob J Ender
Institutions
- University of Vienna (AT)
- University of Victoria (CA)
- BOKU University (AT)
Publication Details
- Journal
- Frontiers in Molecular Biosciences
- Published
- 2024-09-26
- DOI
- https://doi.org/10.3389/fmolb.2024.1470989
- Primary Topic
- Glycosylation and Glycoproteins Research
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- Österreichischen Akademie der Wissenschaften
- Austrian Science Fund
- Hochschuljubiläumsstiftung der Stadt Wien