Journal article

Crystal structure of bacterial succinate: quinone oxidoreductase flavoprotein SdhA in complex with its assembly factor SdhE

Megan J Maher, Anuradha S Herath, Saumya R Udagedara, David A Dougan, Kaye N Truscott

Proceedings of the National Academy of Sciences of the United States of America | NATL ACAD SCIENCES | Published : 2018

Abstract

Succinate:quinone oxidoreductase (SQR) functions in energy metabolism, coupling the tricarboxylic acid cycle and electron transport chain in bacteria and mitochondria. The biogenesis of flavinylated SdhA, the catalytic subunit of SQR, is assisted by a highly conserved assembly factor termed SdhE in bacteria via an unknown mechanism. By using X-ray crystallography, we have solved the structure of Escherichia coli SdhE in complex with SdhA to 2.15-Å resolution. Our structure shows that SdhE makes a direct interaction with the flavin adenine dinucleotide-linked residue His45 in SdhA and maintains the capping domain of SdhA in an "open" conformation. This displaces the catalytic residues of the ..

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University of Melbourne Researchers

Grants

Awarded by Australian Research Council


Funding Acknowledgements

Aspects of this research were undertaken on the Macromolecular Crystallography beamline MX2 at the Australian Synchrotron (Victoria, Australia), and we thank the beamline staff for their enthusiastic and professional support. This work was funded by Australian Research Council Grants DP150104639 (to K.N.T. and D.A.D.), a La Trobe University Full Fee Research Scholarship (to A.S.H.), and a La Trobe University Postgraduate Research Scholarship (to A.S.H.).