Crystal structure of the sucrose phosphorylase from <i>Alteromonas mediterranea</i> shows a loop transition in the active site
Sucrose phosphorylases are essential enzymes regulating sucrose metabolism, and it has been shown that a loop rearrangement is essential to their catalytic cycle. Crystal structures of only six sucrose phosphorylase enzymes are available. Here, we present the crystal structure of a sucrose phosphorylase from a proteobacterium, Alteromonas mediterranea, at 2.15 Å resolution. The available sucrose phosphorylase structures have shown that an important conformational change occurs during the catalytic cycle or upon mutagenesis. Interestingly, our data present clear indications of the two major conformations in the same crystal.
Authors
- Ditte Hededam Welner (ORCID: https://orcid.org/0000-0001-9297-4133)
- Marie Demonceaux (ORCID: https://orcid.org/0000-0002-6090-4007)
- David Tezé (ORCID: https://orcid.org/0000-0002-6865-6108)
- Folmer Fredslund (ORCID: https://orcid.org/0000-0003-0881-1927)
- Marine Goux (ORCID: https://orcid.org/0000-0002-8350-4102)
- Corinne André‐Miral (ORCID: https://orcid.org/0000-0002-3378-2331)
- Bernard Offmann (ORCID: https://orcid.org/0000-0002-6845-5883)
Institutions
- Centre National de la Recherche Scientifique (FR)
- Unité en Sciences Biologiques et Biotechnologies de Nantes (FR)
- Technical University of Denmark (DK)
- Nantes Université (FR)
Publication Details
- Journal
- Acta Crystallographica Section F Structural Biology Communications
- Published
- 2025-05-21
- DOI
- https://doi.org/10.1107/s2053230x25004327
- Primary Topic
- Enzyme Production and Characterization
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- Statens Naturvidenskabelige Forskningsrad
- Novo Nordisk Fonden
- Danish Agency for Science and Higher Education