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

Maher MJ, Herath AS, Udagedara SR, Dougan DA, Truscott KN
Proc Natl Acad Sci U S A 115 2982-2987 (2018)
Cited: 15 times
EuropePMC logo PMID: 29514959

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 succinate dehydrogenase active site by as much as 9.0 Å compared with SdhA in the assembled SQR complex. These data suggest that bacterial SdhE proteins, and their mitochondrial homologs, are assembly chaperones that constrain the conformation of SdhA to facilitate efficient flavinylation while regulating succinate dehydrogenase activity for productive biogenesis of SQR.

Reviews - 6c12 mentioned but not cited (1)

  1. Maturation of the respiratory complex II flavoprotein. Sharma P, Maklashina E, Cecchini G, Iverson TM. Curr Opin Struct Biol 59 38-46 (2019)

Articles - 6c12 mentioned but not cited (5)

  1. Streptococcus gordonii biofilm formation: identification of genes that code for biofilm phenotypes. Loo CY, Corliss DA, Ganeshkumar N. J Bacteriol 182 1374-1382 (2000)
  2. The roles of SDHAF2 and dicarboxylate in covalent flavinylation of SDHA, the human complex II flavoprotein. Sharma P, Maklashina E, Cecchini G, Iverson TM. Proc Natl Acad Sci U S A 117 23548-23556 (2020)
  3. Crystal structure of bacterial succinate:quinone oxidoreductase flavoprotein SdhA in complex with its assembly factor SdhE. Maher MJ, Herath AS, Udagedara SR, Dougan DA, Truscott KN. Proc Natl Acad Sci U S A 115 2982-2987 (2018)
  4. Letter Butterfly-Shaped Diphenylpyrimidine Molecule: Tunable Photophysical Properties by Molecular Self-Assembly Pathways. Choi YJ, Park M, Kim DY, Hsu CH, Hwang SH, Jeong KU. J Phys Chem Lett 6 887-892 (2015)
  5. How an assembly factor enhances covalent FAD attachment to the flavoprotein subunit of complex II. Maklashina E, Iverson TM, Cecchini G. J Biol Chem 298 102472 (2022)


Reviews citing this publication (4)

  1. Mitochondrial complex II and reactive oxygen species in disease and therapy. Hadrava Vanova K, Kraus M, Neuzil J, Rohlena J. Redox Rep 25 26-32 (2020)
  2. The assembly of succinate dehydrogenase: a key enzyme in bioenergetics. Moosavi B, Berry EA, Zhu XL, Yang WC, Yang GF. Cell Mol Life Sci 76 4023-4042 (2019)
  3. Blackout in the powerhouse: clinical phenotypes associated with defects in the assembly of OXPHOS complexes and the mitoribosome. Hock DH, Robinson DRL, Stroud DA. Biochem J 477 4085-4132 (2020)
  4. An evolving view of complex II-noncanonical complexes, megacomplexes, respiration, signaling, and beyond. Iverson TM, Singh PK, Cecchini G. J Biol Chem 299 104761 (2023)

Articles citing this publication (5)

  1. The unassembled flavoprotein subunits of human and bacterial complex II have impaired catalytic activity and generate only minor amounts of ROS. Maklashina E, Rajagukguk S, Iverson TM, Cecchini G. J Biol Chem 293 7754-7765 (2018)
  2. Cryo-EM structure of trimeric Mycobacterium smegmatis succinate dehydrogenase with a membrane-anchor SdhF. Gong H, Gao Y, Zhou X, Xiao Y, Wang W, Tang Y, Zhou S, Zhang Y, Ji W, Yu L, Yu L, Tian C, Lam SM, Shui G, Guddat LW, Wong LL, Wang Q, Rao Z. Nat Commun 11 4245 (2020)
  3. Architecture of the mycobacterial succinate dehydrogenase with a membrane-embedded Rieske FeS cluster. Zhou X, Gao Y, Wang W, Yang X, Yang X, Liu F, Tang Y, Lam SM, Shui G, Yu L, Yu L, Tian C, Guddat LW, Wang Q, Rao Z, Gong H. Proc Natl Acad Sci U S A 118 e2022308118 (2021)
  4. The coenzyme B12 precursor 5,6-dimethylbenzimidazole is a flavin antagonist in Salmonella. Malalasekara L, Escalante-Semerena JC. Microb Cell 10 178-194 (2023)
  5. YgfY Contributes to Stress Tolerance in Shewanella oneidensis Neither as an Antitoxin Nor as a Flavinylation Factor of Succinate Dehydrogenase. Zhang MX, Zheng KL, Tang AG, Hu XX, Guo XX, Wu C, Cheng YY. Microorganisms 9 2316 (2021)


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