Crystal structure of the sucrose phosphorylase from Alteromonas mediterranea shows a loop transition in the active site

2025/05/21 by Folmer Fredslund, Marine Goux, Bernard Offmann +4 · 1 voice
Biochemistry, Genetics and Molecular Biology · Nursing · Materials Science · #Enzyme Production and Characterization #Microbial Metabolites in Food Biotechnology #Enzyme Structure and Function

paper · pdf · doi:10.1107/s2053230x25004327

openalex publication_date 2025/05/21 · openalex created_date 2025/06/23 · openalex updated_date 2026/07/22

Abstract

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.

Citations

• Phasercrystallographic software

Discussions

• The structure of an apo unmutated sucrose phosphorylase from Alteromonas mediterranea shows the presence of two major catalytic conformations in the same crystal @DTUtweet @univnantes @ActaCrystF @IUC [bsky, 2 points, 0 comments]

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