Journal article

Structural and mechanistic insights into a Bacteroides vulgatus retaining N-acetyl-beta-galactosaminidase that uses neighbouring group participation

C Roth, M Petricevic, A John, ED Goddard-Borger, GJ Davies, SJ Williams

CHEMICAL COMMUNICATIONS | ROYAL SOC CHEMISTRY | Published : 2016

Abstract

Bacteroides vulgatus is a member of the human microbiota whose abundance is increased in patients with Crohn's disease. We show that a B. vulgatus glycoside hydrolase from the carbohydrate active enzyme family GH123, BvGH123, is an N-acetyl-β-galactosaminidase that acts with retention of stereochemistry, and, through a 3-D structure in complex with Gal-thiazoline, provide evidence in support of a neighbouring group participation mechanism.

Grants

Awarded by Australian Research Council


Awarded by BBSRC


Awarded by NHMRC IRIISS grant


Awarded by Biotechnology and Biological Sciences Research Council


Funding Acknowledgements

This work was supported by the Australian Research Council (FT130100103), and the BBSRC (BB/K003836/1), and the Ramaciotti Foundation and VESKI with additional support from the Australian Cancer Research Foundation and Victorian State Government Operational Infrastructure Support, NHMRC IRIISS grant 9000220. We thank the Diamond Light Source for access to beamlines I02, I03 and I04 (proposal number mx-9948) that contributed to the results presented here. We also thank Dr Andrew Leech at the Bioscience Technology Facility in the Department of Biology in York for his help with the SEC-MALLS experiments. We are grateful to Dr Johan Turkenburg and Sam Hart for assistance during data collection and Wendy Offen for help with the crystallisation.