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Instruments / Technical Area	Publication Details	Published	Actions
I03-Macromolecular Crystallography I04-Macromolecular Crystallography	Bypassing the requirement for aminoacyl-tRNA by a cyclodipeptide synthase enzyme Christopher Harding , Emmajay Sutherland , Jane G. Hanna , Douglas R. Houston , Clarissa M. Czekster Rsc Chemical Biology 9 DOI: 10.1039/D0CB00142B Diamond Proposal Number(s): [19844] Open Access Show Abstract ▼ Abstract: Cyclodipeptide synthases (CDPSs) produce a variety of cyclic dipeptide products by utilising two aminoacylated tRNA substrates. We sought to investigate the minimal requirements for substrate usage in this class of enzymes as the relationship between CDPSs and their substrates remains elusive. Here, we investigated the Bacillus thermoamylovorans enzyme, BtCDPS, which synthesises cyclo(L-Leu–L-Leu). We systematically tested where specificity arises and, in the process, uncovered small molecules (activated amino esters) that will suffice as substrates, although catalytically poor. We solved the structure of BtCDPS to 1.7 Å and combining crystallography, enzymatic assays and substrate docking experiments propose a model for how the minimal substrates interact with the enzyme. This work is the first report of a CDPS enzyme utilizing a molecule other than aa-tRNA as a substrate; providing insights into substrate requirements and setting the stage for the design of improved simpler substrates.	Jan 2021
I03-Macromolecular Crystallography	Glycosylated cyclophellitol-derived activity-based probes and inhibitors for cellulases Casper De Boer , Nicholas G. S. Mcgregor , Evert Peterse , Sybrin P. Schröder , Bogdan I. Florea , Jianbing Jiang , Jos Reijngoud , Arthur F. J. Ram , Gilles P. Van Wezel , Gijsbert A. Van Der Marel , Jeroen D. C. Codée , Herman S. Overkleeft , Gideon Davies Rsc Chemical Biology 25 DOI: 10.1039/D0CB00045K Diamond Proposal Number(s): [18598] Open Access Show Abstract ▼ Abstract: Cellulases and related β-1,4-glucanases are essential components of lignocellulose-degrading enzyme mixtures. The detection of β-1,4-glucanase activity typically relies on monitoring the breakdown of purified lignocellulose-derived substrates or synthetic chromogenic substrates, limiting the activities which can be detected and complicating the tracing of activity back to specific components within complex enzyme mixtures. As a tool for the rapid detection and identification of β-1,4-glucanases, a series of glycosylated cyclophellitol inhibitors mimicking β-1,4-glucan oligosaccharides have been synthesised. These compounds are highly efficient inhibitors of HiCel7B, a well-known GH7 endo-β-1,4-glucanase. An elaborated activity-based probe facilitated the direct detection and identification of β-1,4-glucanases within a complex fungal secretome without any detectable cross-reactivity with β-D-glucosidases. These probes and inhibitors add valuable new capacity to the growing toolbox of cyclophellitol-derived probes for the activity-based profiling of biomass-degrading enzymes.	Jul 2020

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