Related Experiment Video
Updated: Sep 18, 2025

Modeling an Enzyme Active Site using Molecular Visualization Freeware
Published on: December 25, 2021
Crystal structure of the sucrose phosphorylase from Alteromonas mediterranea shows a loop transition in the active
Folmer Fredslund1, Marine Goux2, Bernard Offmann2
1DTU Biosustain, Technical University of Denmark, Kongens Lyngby, Hovedstaden, Denmark.
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.
More Related Videos
13:35Structural Biology and Analytical Chemistry Approaches for Characterizing C-Glycoside Metabolic Enzymes in Human Gut Microbiota
Published on: May 23, 2025
13:34Production, Crystallization and Structure Determination of C. difficile PPEP-1 via Microseeding and Zinc-SAD
Published on: December 30, 2016
Related Concept Videos
ATP Synthase: Structure
ATP Synthase: Mechanism
Cooperative Allosteric Transitions
Allosteric Proteins-ATCase
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
ATP Energy Storage and Release
One example of energy coupling using ATP involves a...
Ligand Binding and Linkage