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Structural insights into enzyme-substrate interaction and characterization of enzymatic intermediates of organic hydroperoxide resistance protein from Xylella fastidiosa.

Oliveira MA, Guimarães BG, Cussiol JR, Medrano FJ, Gozzo FC, Netto LE
J Mol Biol 359 433-45 (2006)
Cited: 21 times
EuropePMC logo PMID: 16631787

Abstract

Organic hydroperoxide resistance proteins (Ohr) belong to a family of proteins that possess thiol-dependent peroxidase activity endowed by reactive cysteine residues able to reduce peroxides. The crystal structure of Ohr from Xylella fastidiosa in complex with polyethylene glycol, providing insights into enzyme-substrate interactions is described herein. In addition, crystallographic studies, molecular modeling and biochemical assays also indicated that peroxides derived from long chain fatty acids could be the biological substrates of Ohr. Because different oxidation states of the reactive cysteine were present in the Ohr structures from X. fastidiosa, Pseudomonas aeruginosa and Deinococcus radiodurans it was possible to envisage a set of snapshots along the coordinate of the enzyme-catalyzed reaction. The redox intermediates of X. fastidiosa Ohr observed in the crystals were further characterized in solution by electrospray ionization mass spectrometry and by biochemical approaches. In this study, the formation of an intramolecular disulfide bond and oxidative inactivation through the formation of a sulfonic acid derivative was unequivocally demonstrated for the first time. Because Ohr proteins are exclusively present in bacteria, they may represent promising targets for therapeutical drugs. In this regard, the structural and functional analyses of Ohr presented here might be very useful.

Articles - 1zb9 mentioned but not cited (1)

  1. Structural insights on the efficient catalysis of hydroperoxide reduction by Ohr: Crystallographic and molecular dynamics approaches. Piccirillo E, Alegria TGP, Discola KF, Cussiol JRR, Domingos RM, de Oliveira MA, Rezende L, Netto LES, Amaral AT. PLoS ONE 13 e0196918 (2018)


Reviews citing this publication (3)

  1. Living in two worlds: the plant and insect lifestyles of Xylella fastidiosa. Chatterjee S, Almeida RP, Lindow S. Annu Rev Phytopathol 46 243-271 (2008)
  2. Why do bacteria use so many enzymes to scavenge hydrogen peroxide? Mishra S, Imlay J. Arch. Biochem. Biophys. 525 145-160 (2012)
  3. Reactive cysteine in proteins: protein folding, antioxidant defense, redox signaling and more. Netto LE, de Oliveira MA, Monteiro G, Demasi AP, Cussiol JR, Discola KF, Demasi M, Silva GM, Alves SV, Faria VG, Horta BB. Comp. Biochem. Physiol. C Toxicol. Pharmacol. 146 180-193 (2007)

Articles citing this publication (17)

  1. Functional site profiling and electrostatic analysis of cysteines modifiable to cysteine sulfenic acid. Salsbury FR, Knutson ST, Poole LB, Fetrow JS. Protein Sci. 17 299-312 (2008)
  2. Organic hydroperoxide resistance protein and ergothioneine compensate for loss of mycothiol in Mycobacterium smegmatis mutants. Ta P, Buchmeier N, Newton GL, Rawat M, Fahey RC. J. Bacteriol. 193 1981-1990 (2011)
  3. Macrophage replication screen identifies a novel Francisella hydroperoxide resistance protein involved in virulence. Llewellyn AC, Jones CL, Napier BA, Bina JE, Weiss DS. PLoS ONE 6 e24201 (2011)
  4. Ohr (organic hydroperoxide resistance protein) possesses a previously undescribed activity, lipoyl-dependent peroxidase. Cussiol JR, Alegria TG, Szweda LI, Netto LE. J. Biol. Chem. 285 21943-21950 (2010)
  5. The crystal structure of the periplasmic domain of the Escherichia coli membrane protein insertase YidC contains a substrate binding cleft. Ravaud S, Stjepanovic G, Wild K, Sinning I. J Biol Chem 283 9350-9358 (2008)
  6. Role of glutaredoxin 2 and cytosolic thioredoxins in cysteinyl-based redox modification of the 20S proteasome. Silva GM, Netto LE, Discola KF, Piassa-Filho GM, Pimenta DC, Bárcena JA, Demasi M. FEBS J. 275 2942-2955 (2008)
  7. Structural and functional characterization of an organic hydroperoxide resistance protein from Mycoplasma gallisepticum. Jenkins C, Samudrala R, Geary SJ, Djordjevic SP. J. Bacteriol. 190 2206-2216 (2008)
  8. Human carotid lesion linoleic acid hydroperoxide inhibits paraoxonase 1 (PON1) activity via reaction with PON1 free sulfhydryl cysteine 284. Tavori H, Aviram M, Khatib S, Musa R, Mannheim D, Karmeli R, Vaya J. Free Radic. Biol. Med. 50 148-156 (2011)
  9. Analysis of the organic hydroperoxide response of Chromobacterium violaceum reveals that OhrR is a cys-based redox sensor regulated by thioredoxin. da Silva Neto JF, Negretto CC, Netto LE. PLoS ONE 7 e47090 (2012)
  10. Ohr plays a central role in bacterial responses against fatty acid hydroperoxides and peroxynitrite. Alegria TG, Meireles DA, Cussiol JR, Hugo M, Trujillo M, de Oliveira MA, Miyamoto S, Queiroz RF, Valadares NF, Garratt RC, Radi R, Di Mascio P, Augusto O, Netto LE. Proc. Natl. Acad. Sci. U.S.A. 114 E132-E141 (2017)
  11. The Mycoplasma genitalium MG_454 gene product resists killing by organic hydroperoxides. Saikolappan S, Sasindran SJ, Yu HD, Baseman JB, Dhandayuthapani S. J. Bacteriol. 191 6675-6682 (2009)
  12. A 14.7 kDa protein from Francisella tularensis subsp. novicida (named FTN_1133), involved in the response to oxidative stress induced by organic peroxides, is not endowed with thiol-dependent peroxidase activity. Meireles Dde A, Alegria TG, Alves SV, Arantes CR, Netto LE. PLoS ONE 9 e99492 (2014)
  13. Cloning, expression, purification and characterization of recombinant glutathione-S-transferase from Xylella fastidiosa. Travensolo RF, Garcia W, Muniz JR, Caruso CS, Lemos EG, Carrilho E, Araújo AP. Protein Expr. Purif. 59 153-160 (2008)
  14. Large-scale computational discovery and analysis of virus-derived microbial nanocompartments. Andreas MP, Giessen TW. Nat Commun 12 4748 (2021)
  15. Functional and evolutionary characterization of Ohr proteins in eukaryotes reveals many active homologs among pathogenic fungi. Meireles DA, Domingos RM, Gaiarsa JW, Ragnoni EG, Bannitz-Fernandes R, da Silva Neto JF, de Souza RF, Netto LES. Redox Biol 12 600-609 (2017)
  16. Ohr and OhrR Are Critical for Organic Peroxide Resistance and Symbiosis in Azorhizobium caulinodans ORS571. Si Y, Guo D, Deng S, Lu X, Zhu J, Rao B, Cao Y, Jiang G, Yu D, Zhong Z, Zhu J. Genes (Basel) 11 (2020)
  17. Transcriptomic response of Ralstonia solanacearum to antimicrobial Pseudomonas fluorescens SN15-2 metabolites. Lou H, Wang X, Chen J, Wang B, Wang W. Can. J. Microbiol. 64 816-825 (2018)


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