8HU4

Limosilactobacillus reuteri N1 GtfB

Summary for 8HU4

• Entry DOI: 10.2210/pdb8hu4/pdb
• Descriptor: dextransucrase, SODIUM ION, CITRIC ACID, ... (5 entities in total)
• Functional Keywords: glucanotransferase, carbohydrate-active enzyme, transferase
• Biological source: Limosilactobacillus reuteri (Lactobacillus reuteri)
• Total number of polymer chains: 2
• Total formula weight: 185430.69

Authors

Dong, J.J.,Bai, Y.X. (deposition date: 2022-12-22, release date: 2023-12-27, Last modification date: 2024-03-27)

Primary citation

Dong, J.,Bai, Y.,Wang, Q.,Chen, Q.,Li, X.,Wang, Y.,Ji, H.,Meng, X.,Pijning, T.,Svensson, B.,Dijkhuizen, L.,Abou Hachem, M.,Jin, Z.
Insights into the Structure-Function Relationship of GH70 GtfB alpha-Glucanotransferases from the Crystal Structure and Molecular Dynamic Simulation of a Newly Characterized Limosilactobacillus reuteri N1 GtfB Enzyme.
J.Agric.Food Chem., 72:5391-5402, 2024

PubMed Abstract: α-Glucanotransferases of the CAZy family GH70 convert starch-derived donors to industrially important α-glucans. Here, we describe characteristics of a novel GtfB-type 4,6-α-glucanotransferase of high enzyme activity (60.8 U mg) from N1 (LrN1 GtfB), which produces surprisingly large quantities of soluble protein in heterologous expression (173 mg pure protein per L of culture) and synthesizes the reuteran-like α-glucan with (α1 → 6) linkages in linear chains and branch points. Protein structural analysis of LrN1 GtfB revealed the potential crucial residues at subsites -2∼+2, particularly H265, Y214, and R302, in the active center as well as previously unidentified surface binding sites. Furthermore, molecular dynamic simulations have provided unprecedented insights into linkage specificity hallmarks of the enzyme. Therefore, LrN1 GtfB represents a potent enzymatic tool for starch conversion, and this study promotes our knowledge on the structure-function relationship of GH70 GtfB α-glucanotransferases, which might facilitate the production of tailored α-glucans by enzyme engineering in future.

PubMed: 38427803
DOI: 10.1021/acs.jafc.4c00104

Experimental method

X-RAY DIFFRACTION (2.76 Å)