2v21 › Citations

The dodecin from Thermus thermophilus, a bifunctional cofactor storage protein.

Meissner B, Schleicher E, Weber S, Essen LO
J Biol Chem 282 33142-54 (2007)
Related entries: 2ux9, 2v18, 2v19

Cited: 16 times
EuropePMC logo PMID: 17855371

Abstract

Dodecins are so far the smallest known flavoproteins (68-71 amino acids) and are most likely involved in prokaryotic flavin storage. The dodecin monomers adopt a simple betaalphabetabeta-fold and assemble to hollow sphere-like dodecameric complexes. Flavin binding by the dodecin from Thermus thermophilus showed a 1:1 stoichiometry and apparent dissociation constants in the submicromolar to nanomolar range as characterized by isothermal titration calorimetry and fluorescence titrations. The x-ray structures of the flavin-prebound and FMN-reconstituted state of the T. thermophilus dodecin revealed binding of FMN dimers in a novel si-si- rather than the re-re- orientation of their isoalloxazine moieties as found before in an archaeal dodecin. Electron paramagnetic resonance studies demonstrated that upon reduction the excess electron is localized only on one flavin, thus making dodecin-bound flavins highly refractory to redox chemistry. Besides FMN dimers, trimers of coenzyme A are additionally bound to this eubacterial dodecin along the 3-fold symmetry face II of the dodecin complex. Therefore, dodecins can act as bifunctional cofactor storage proteins that sequester catalytic cofactors in prokaryotes very efficiently in an aggregated and unreactive state.

Reviews citing this publication (1)

  1. A survey of the year 2007 literature on applications of isothermal titration calorimetry. Bjelić S, Jelesarov I. J Mol Recognit 21 289-312 (2008)

Articles citing this publication (15)

  1. In vivo generation of flavoproteins with modified cofactors. Mathes T, Vogl C, Stolz J, Hegemann P. J Mol Biol 385 1511-1518 (2009)
  2. Unusual arginine formations in protein function and assembly: rings, strings, and stacks. Neves MA, Yeager M, Abagyan R. J Phys Chem B 116 7006-7013 (2012)
  3. Dodecin is the key player in flavin homeostasis of archaea. Grininger M, Staudt H, Johansson P, Wachtveitl J, Oesterhelt D. J Biol Chem 284 13068-13076 (2009)
  4. Ultrafast excited-state deactivation of flavins bound to dodecin. Staudt H, Oesterhelt D, Grininger M, Wachtveitl J. J Biol Chem 287 17637-17644 (2012)
  5. Blue-light-triggered photorelease of active chemicals captured by the flavoprotein dodecin. Nöll G, Trawöger S, von Sanden-Flohe M, Dick B, Grininger M. Chembiochem 10 834-837 (2009)
  6. Structural and biophysical characterization of Mycobacterium tuberculosis dodecin Rv1498A. Liu F, Xiong J, Kumar S, Yang C, Ge S, Li S, Xia N, Swaminathan K. J Struct Biol 175 31-38 (2011)
  7. Electrochemical switching of the flavoprotein dodecin at gold surfaces modified by flavin-DNA hybrid linkers. Grininger M, Nöll G, Trawöger S, Sinner EK, Oesterhelt D. Biointerphases 3 51-58 (2008)
  8. Photoinduced damage of AsLOV2 domain is accompanied by increased singlet oxygen production due to flavin dissociation. Petrenčáková M, Filandr F, Hovan A, Yassaghi G, Man P, Kožár T, Schwer MS, Jancura D, Plückthun A, Novák P, Miškovský P, Bánó G, Sedlák E. Sci Rep 10 4119 (2020)
  9. Chemical engineering of Mycobacterium tuberculosis dodecin hybrids. Vinzenz X, Grosse W, Linne U, Meissner B, Essen LO. Chem Commun (Camb) 47 11071-11073 (2011)
  10. Crystal structure of calcium dodecin (Rv0379), from Mycobacterium tuberculosis with a unique calcium-binding site. Arockiasamy A, Aggarwal A, Savva CG, Holzenburg A, Sacchettini JC. Protein Sci 20 827-833 (2011)
  11. Spectroscopic evidence for direct flavin-flavin contact in a bifurcating electron transfer flavoprotein. Duan HD, Mohamed-Raseek N, Miller AF. J Biol Chem 295 12618-12634 (2020)
  12. Reverse structural genomics: an unusual flavin-binding site in a putative protease from Bacteroides thetaiotaomicron. Knaus T, Eger E, Koop J, Stipsits S, Kinsland CL, Ealick SE, Macheroux P. J Biol Chem 287 27490-27498 (2012)
  13. Characterization of the small flavin-binding dodecin in the roseoflavin producer Streptomyces davawensis. Ludwig P, Sévin DC, Busche T, Kalinowski J, Bourdeaux F, Grininger M, Mack M. Microbiology (Reading) 164 908-919 (2018)
  14. Dodecin as carrier protein for immunizations and bioengineering applications. Bourdeaux F, Kopp Y, Lautenschläger J, Gößner I, Besir H, Vabulas RM, Grininger M. Sci Rep 10 13297 (2020)
  15. M. bovis BCG Moreau N-Terminal Loss Leads to a Less Stable Dodecin With Lower Flavin Binding Capacity. Schwarz MGA, Luzes BGC, Correa PR, da Silva-Gonçalves AJ, Machado LA, Guimarães ACR, Mendonça-Lima L. Front Cell Infect Microbiol 11 658888 (2021)


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