Journal article
The sulfoquinovosyl glycerol binding protein SmoF binds and accommodates plant sulfolipids
AJD Snow, M Sharma, JP Lingford, Y Zhang, JWY Mui, R Epa, ED Goddard-Borger, SJ Williams, GJ Davies
Current Research in Structural Biology | Published : 2022
Abstract
Sulfoquinovose (SQ) is the anionic headgroup of the ubiquitous plant sulfolipid, sulfoquinovosyl diacylglycerol (SQDG). SQDG can undergo delipidation to give sulfoquinovosyl glycerol (SQGro) and further glycoside cleavage to give SQ, which can be metabolized through microbial sulfoglycolytic pathways. Exogenous SQDG metabolites are imported into bacteria through membrane spanning transporter proteins. The recently discovered sulfoglycolytic sulfoquinovose monooxygenase (sulfo-SMO) pathway in Agrobacterium tumefaciens features a periplasmic sulfoquinovosyl glycerol binding protein, SmoF, and an ATP-binding cassette (ABC) transporter. Here, we use X-ray crystallography, differential scanning f..
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Awarded by Australian Cancer Research Foundation
Funding Acknowledgements
GJD is supported by the Royal Society Ken Murray Research Professorship. MS and AS were funded by the Leverhulme Trust (grant RPG-2017-190) and MS subsequently by the Biotechnology and Biological Sciences Research Council (BB/W003805/1) . SJW is supported by the Australian Research Council (DP180101957 and DP210100233) . EDGB is supported by the Brian M. Davis Charitable Foundation Centenary Fellowship, National Health and Medical Research Council of Australia (NHMRC) project grants GNT1139546, GNT1139549 and GNT2000517, and acknowledges support from The Walter and Eliza Hall Institute of Medical Research, the Australian Cancer Research Fund and a Victorian State Government Operational Infrastructure support grant.