5JVV

Crystal structure and characterization an elongating GH family 16 beta-1,3-glucosyltransferase

Summary for 5JVV

• Entry DOI: 10.2210/pdb5jvv/pdb
• Descriptor: beta-1,3-glucosyltransferase (2 entities in total)
• Functional Keywords: glucoside hydrolase, beta-1, 3-glucosyltransferase, transferase
• Biological source: Paecilomyces sp. J18 (Paecilomyces thermophila J18)
• Total number of polymer chains: 2
• Total formula weight: 65081.57

Authors

Qin, Z.,Yan, Q.,Yang, S.,Jiang, Z. (deposition date: 2016-05-11, release date: 2016-12-14, Last modification date: 2024-11-06)

Primary citation

Qin, Z.,Yang, S.,Zhao, L.,You, X.,Yan, Q.,Jiang, Z.
Catalytic Mechanism of a Novel Glycoside Hydrolase Family 16 "Elongating" beta-Transglycosylase
J. Biol. Chem., 292:1666-1678, 2017

PubMed Abstract: Carbohydrates are complex macromolecules in biological metabolism. Enzymatic synthesis of carbohydrates is recognized as a powerful tool to overcome the problems associated with large scale synthesis of carbohydrates. Novel enzymes with significant transglycosylation ability are still in great demand in glycobiology studies. Here we report a novel glycoside hydrolase family 16 "elongating" β-transglycosylase from Paecilomyces thermophila (PtBgt16A), which efficiently catalyzes the synthesis of higher polymeric oligosaccharides using β-1,3/1,4-oligosaccharides as donor/acceptor substrates. Further structural information reveals that PtBgt16A has a binding pocket around the -1 subsite. The catalytic mechanism of PtBgt16A is partly similar to an exo-glycoside hydrolase, which cleaves the substrate from the non-reducing end one by one. However, PtBgt16A releases the reducing end product and uses the remainder glucosyl as a transglycosylation donor. This catalytic mechanism has similarity with the catalytic mode of amylosucrase, which catalyzes the transglycosylation products gradually extend by one glucose unit. PtBgt16A thus has the potential to be a tool enzyme for the enzymatic synthesis of new β-oligosaccharides and glycoconjugates.

PubMed: 27956553
DOI: 10.1074/jbc.M116.762419

Experimental method

X-RAY DIFFRACTION (1.589 Å)