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Structural and kinetic properties of lumazine synthase isoenzymes in the order Rhizobiales.

Klinke S, Zylberman V, Bonomi HR, Haase I, Guimarães BG, Braden BC, Bacher A, Fischer M, Goldbaum FA
J Mol Biol 373 664-80 (2007)
Related entries: 2f59, 2i0f, 2obx

Cited: 13 times
EuropePMC logo PMID: 17854827

Abstract

6,7-Dimethyl-8-ribityllumazine synthase (lumazine synthase; LS) catalyzes the penultimate step in the biosynthesis of riboflavin in plants and microorganisms. This protein is known to exhibit different quaternary assemblies between species, existing as free pentamers, decamers (dimers of pentamers) and icosahedrally arranged dodecamers of pentamers. A phylogenetic analysis on eubacterial, fungal and plant LSs allowed us to classify them into two categories: Type I LSs (pentameric or icosahedral) and Type II LSs (decameric). The Rhizobiales represent an order of alpha-proteobacteria that includes, among others, the genera Mesorhizobium, Agrobacterium and Brucella. Here, we present structural and kinetic studies on several LSs from Rhizobiales. Interestingly, Mesorhizobium and Brucella encode both a Type-I LS and a Type-II LS called RibH1 and RibH2, respectively. We show that Type II LSs appear to be almost inactive, whereas Type I LSs present a highly variable catalytic activity according to the genus. Additionally, we have solved four RibH1/RibH2 crystallographic structures from the genera Mesorhizobium and Brucella. The relationship between the active-site architecture and catalytic properties in these isoenzymes is discussed, and a model that describes the enzymatic behavior is proposed. Furthermore, sequence alignment studies allowed us to extend our results to the genus Agrobacterium. Our results suggest that the selective pressure controlling the riboflavin pathway favored the evolution of catalysts with low reaction rates, since the excess of flavins in the intracellular pool in Rhizobiales could act as a negative factor when these bacteria are exposed to oxidative or nitrosative stress.

Reviews citing this publication (4)

  1. Genetic control of biosynthesis and transport of riboflavin and flavin nucleotides and construction of robust biotechnological producers. Abbas CA, Sibirny AA. Microbiol Mol Biol Rev 75 321-360 (2011)
  2. Biosynthesis of vitamin B2: Structure and mechanism of riboflavin synthase. Fischer M, Bacher A. Arch Biochem Biophys 474 252-265 (2008)
  3. The lumazine synthase/riboflavin synthase complex: shapes and functions of a highly variable enzyme system. Ladenstein R, Fischer M, Bacher A. FEBS J 280 2537-2563 (2013)
  4. Biosynthesis of vitamin B2: a unique way to assemble a xylene ring. Fischer M, Bacher A. Chembiochem 12 670-680 (2011)

Articles citing this publication (9)

  1. 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)
  2. An atypical riboflavin pathway is essential for Brucella abortus virulence. Bonomi HR, Marchesini MI, Klinke S, Ugalde JE, Zylberman V, Ugalde RA, Comerci DJ, Goldbaum FA. PLoS One 5 e9435 (2010)
  3. Proteomics-based confirmation of protein expression and correction of annotation errors in the Brucella abortus genome. Lamontagne J, Béland M, Forest A, Côté-Martin A, Nassif N, Tomaki F, Moriyón I, Moreno E, Paramithiotis E. BMC Genomics 11 300 (2010)
  4. Stabilization of the SARS-CoV-2 Spike Receptor-Binding Domain Using Deep Mutational Scanning and Structure-Based Design. Ellis D, Brunette N, Crawford KHD, Walls AC, Pham MN, Chen C, Herpoldt KL, Fiala B, Murphy M, Pettie D, Kraft JC, Malone KD, Navarro MJ, Ogohara C, Kepl E, Ravichandran R, Sydeman C, Ahlrichs M, Johnson M, Blackstone A, Carter L, Starr TN, Greaney AJ, Lee KK, Veesler D, Bloom JD, King NP. Front Immunol 12 710263 (2021)
  5. Antigen- and scaffold-specific antibody responses to protein nanoparticle immunogens. Kraft JC, Pham MN, Shehata L, Brinkkemper M, Boyoglu-Barnum S, Sprouse KR, Walls AC, Cheng S, Murphy M, Pettie D, Ahlrichs M, Sydeman C, Johnson M, Blackstone A, Ellis D, Ravichandran R, Fiala B, Wrenn S, Miranda M, Sliepen K, Brouwer PJM, Antanasijevic A, Veesler D, Ward AB, Kanekiyo M, Pepper M, Sanders RW, King NP. Cell Rep Med 3 100780 (2022)
  6. Sensing the dissociation of a polymeric enzyme by means of an engineered intrinsic probe. Ainciart N, Zylberman V, Craig PO, Nygaard D, Bonomi HR, Cauerhff AA, Goldbaum FA. Proteins 79 1079-1088 (2011)
  7. Asymmetric bifunctional protein nanoparticles through redesign of self-assembly. Sosa S, Rossi AH, Szalai AM, Klinke S, Rinaldi J, Farias A, Berguer PM, Nadra AD, Stefani FD, Goldbaum FA, Bonomi HR. Nanoscale Adv 1 1833-1846 (2019)
  8. Improvement of Cellulomonas fimi endoglucanase CenA by multienzymatic display on a decameric structural scaffold. Iglesias Rando MR, Gorojovsky N, Zylberman V, Goldbaum FA, Craig PO. Appl Microbiol Biotechnol 107 4261-4274 (2023)
  9. Process development of a SARS-CoV-2 nanoparticle vaccine. Martinez-Cano D, Ravichandran R, Le H, Wong HE, Jagannathan B, Liu EJ, Bailey W, Yang J, Matthies K, Barkhordarian H, Shah B, Srinivasan N, Zhang J, Hsu A, Wypych J, Stevens J, Piedmonte DM, Miranda LP, Carter L, Murphy M, King NP, Soice N. Process Biochem 129 241-256 (2023)


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