Reversibility of a Point Mutation Induced Domain Shift: Expanding the Conformational Space of a Sucrose Phosphorylase
Please always quote using this URN: urn:nbn:de:bvb:20-opus-224845
- Despite their popularity as enzyme engineering targets structural information about Sucrose Phosphorylases remains scarce. We recently clarified that the Q345F variant of Bifidobacterium adolescentis Sucrose Phosphorylase is able to accept large polyphenolic substrates like resveratrol via a domain shift. Here we present a crystal structure of this variant in a conformation suitable for the accommodation of the donor substrate sucrose in excellent agreement with the wild type structure. Remarkably, this conformation does not feature theDespite their popularity as enzyme engineering targets structural information about Sucrose Phosphorylases remains scarce. We recently clarified that the Q345F variant of Bifidobacterium adolescentis Sucrose Phosphorylase is able to accept large polyphenolic substrates like resveratrol via a domain shift. Here we present a crystal structure of this variant in a conformation suitable for the accommodation of the donor substrate sucrose in excellent agreement with the wild type structure. Remarkably, this conformation does not feature the previously observed domain shift which is therefore reversible and part of a dynamic process rather than a static phenomenon. This crystallographic snapshot completes our understanding of the catalytic cycle of this useful variant and will allow for a more rational design of further generations of Sucrose Phosphorylase variants.…
Author: | Michael Kraus, Clemens Grimm, Jürgen Seibel |
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URN: | urn:nbn:de:bvb:20-opus-224845 |
Document Type: | Journal article |
Faculties: | Fakultät für Biologie / Theodor-Boveri-Institut für Biowissenschaften |
Fakultät für Chemie und Pharmazie / Institut für Organische Chemie | |
Language: | English |
Parent Title (English): | Scientific Reports |
Year of Completion: | 2018 |
Volume: | 8 |
Article Number: | 10490 |
Source: | Scientific Reports (2018) 8:10490. https://doi.org/10.1038/s41598-018-28802-2 |
DOI: | https://doi.org/10.1038/s41598-018-28802-2 |
Dewey Decimal Classification: | 5 Naturwissenschaften und Mathematik / 54 Chemie / 547 Organische Chemie |
5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie | |
Tag: | X-ray crystallography; biocatalysis |
Release Date: | 2024/07/11 |
Licence (German): | CC BY: Creative-Commons-Lizenz: Namensnennung 4.0 International |