Mechanisms of redundancy and specificity of the Aspergillus fumigatus Crh transglycosylases

Wenxia Fang, Ana Belén Sanz, Sergio Galan Bartual, Bin Wang, Andrew T. Ferenbach, Vladimír Farkaš, Ramon Hurtado-Guerrero, Javier Arroyo () and Daan M. F. Aalten ()
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Wenxia Fang: University of Dundee
Ana Belén Sanz: IRYCIS
Sergio Galan Bartual: University of Dundee
Bin Wang: Guangxi Academy of Sciences
Andrew T. Ferenbach: University of Dundee
Vladimír Farkaš: Center for Glycomics, Slovak Academy of Sciences
Ramon Hurtado-Guerrero: University of Zaragoza, BIFI-IQFR (CSIC)
Javier Arroyo: IRYCIS
Daan M. F. Aalten: University of Dundee

Nature Communications, 2019, vol. 10, issue 1, 1-10

Abstract: Abstract Fungal cell wall synthesis is achieved by a balance of glycosyltransferase, hydrolase and transglycosylase activities. Transglycosylases strengthen the cell wall by forming a rigid network of crosslinks through mechanisms that remain to be explored. Here we study the function of the Aspergillus fumigatus family of five Crh transglycosylases. Although crh genes are dispensable for cell viability, simultaneous deletion of all genes renders cells sensitive to cell wall interfering compounds. In vitro biochemical assays and localisation studies demonstrate that this family of enzymes functions redundantly as transglycosylases for both chitin-glucan and chitin-chitin cell wall crosslinks. To understand the molecular basis of this acceptor promiscuity, we solved the crystal structure of A. fumigatus Crh5 (AfCrh5) in complex with a chitooligosaccharide at the resolution of 2.8 Å, revealing an extensive elongated binding cleft for the donor (−4 to −1) substrate and a short acceptor (+1 to +2) binding site. Together with mutagenesis, the structure suggests a “hydrolysis product assisted” molecular mechanism favouring transglycosylation over hydrolysis.

Date: 2019
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DOI: 10.1038/s41467-019-09674-0

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