Journal article
Capture-and-release of a sulfoquinovose-binding protein on sulfoquinovose-modified agarose
Thimali Arumapperuma, Alexander JD Snow, Mihwa Lee, Mahima Sharma, Yunyang Zhang, James P Lingford, Ethan D Goddard-Borger, Gideon J Davies, Spencer J Williams
Organic and Biomolecular Chemistry | Royal Society of Chemistry | Published : 2024
DOI: 10.1039/d4ob00307a
Abstract
The solute-binding protein (SBP) components of periplasmic binding protein-dependent ATP-binding cassette (ABC)-type transporters often possess exquisite selectivity for their cognate ligands. Maltose binding protein (MBP), the best studied of these SBPs, has been extensively used as a fusion partner to enable the affinity purification of recombinant proteins. However, other SBPs and SBP-ligand based affinity systems remain underexplored. The sulfoquinovose-binding protein SmoF, is a substrate-binding protein component of the ABC transporter cassette in Agrobacterium tumefaciens involved in importing sulfoquinovose (SQ) and its derivatives for SQ catabolism. Here, we show that SmoF binds wit..
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Grants
Awarded by Australian Cancer Research Foundation
Awarded by Australian Research Council
Awarded by Biotechnology and Biological Sciences Research Council
Awarded by Royal Society
Funding Acknowledgements
This work was supported by the Australian Research Council (DP210100233, DP210100235, DP240100126), the Biotechnology and Biological Sciences Research Council (BB/W003805/1), Leverhulme Trust (RPG-2017-190), and the Royal Society (Ken Murray Research Professorship to G. J. D.). E. D. G.-B. acknowledges support from The Walter and Eliza Hall Institute of Medical Research, National Health and Medical Research Council of Australia (NHMRC) Ideas grant GNT2027601, the Australian Cancer Research Fund, and a Rebecca Cooper Fellowship. We acknowledge Dr Johan P. Turkenburg and Sam Hart for assistance with X-ray data collection; the staff of the Diamond Light Source (U.K.) for provision of IO3 and IO4 beamline facilities (proposal numbers mx-18598).