Sandbox GGC1

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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
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This is the structure of the yeast CsNMO. <scene name='75/752263/Alpha_beta_sheets/1'>This view</scene> shows the alpha helixes and beta pleaded sheets of nitronate monooxygenase. There are eight parallel beta strands that are depicted in that are surrounded by eight alpha helixes.
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This is the structure of the yeast CsNMO. <scene name='75/752263/Alpha_beta_sheets/1'>This view</scene> shows the alpha helixes and beta pleated sheets of nitronate monooxygenase. There is eight parallel beta pleaded strands that are depicted in pink surrounded by eight alpha helixes in blue.
FMN Binding site is formed with hydrogen bonds with main chain amino acids of G240, G261, and T262. <scene name='75/752263/Fmn_binding_site/1'>This is a view of the FMN Binding Site with labeled amino acid residues.</scene>
FMN Binding site is formed with hydrogen bonds with main chain amino acids of G240, G261, and T262. <scene name='75/752263/Fmn_binding_site/1'>This is a view of the FMN Binding Site with labeled amino acid residues.</scene>

Revision as of 21:58, 22 April 2018

Crystal Structure of yeast nitronate monooxygenase from Cyberlindera saturnas

Caption for this structure

Drag the structure with the mouse to rotate

References

  1. ↑ Huerta C, Borek D, Machius M, Grishin NV, Zhang H. Structure and Mechanism of a Eukaryotic FMN Adenylyltransferase. Journal of molecular biology. 2009;389(2):388-400. doi:10.1016/j.jmb.2009.04.022.
  2. ↑ Francis K, Nishino SF, Spain JC, Gadda G. A novel activity for fungal nitronate monooxygenase: detoxification of the metabolic inhibitor propionate-3-nitronate. Arch Biochem Biophys. 2012;521(1–2):84–89.
  3. ↑ Gadda G, Francis K. Nitronate monooxygenase, a model for anionic flavin semiquinone intermediates in oxidative catalysis. Arch Biochem Biophys. 2010;493(1):53–61.
  4. ↑ Salvi F, Agniswamy J, Yuan H, et al. The combined structural and kinetic characterization of a bacterial nitronate monooxygenase from Pseudomonas aeruginosa PAO1 establishes NMO class I and II.J Biol Chem. 2014;289(34):23764–23775.
  5. ↑ Salvi F, Agniswamy J, Yuan H, et al. The combined structural and kinetic characterization of a bacterial nitronate monooxygenase from Pseudomonas aeruginosa PAO1 establishes NMO class I and II.J Biol Chem. 2014;289(34):23764–23775.
  6. ↑ Smitherman C, Gadda G. Evidence for a transient peroxynitro acid in the reaction catalyzed by nitronate monooxygenase with propionate 3-nitronate. Biochemistry. 2013;52(15):2694–2704.
  7. ↑ Hipkin CR, Simpson DJ, Wainwright SJ, Salem MA. Nitrification by plants that also fix nitrogen. Nature. 2004;430(6995):98–101
  8. ↑ Francis K, Smitherman C, Nishino SF, Spain JC, Gadda G. The biochemistry of the metabolic poison propionate 3-nitronate and its conjugate acid, 3-nitropropionate. IUBMB Life. 2013;65(9):759–768.
  9. ↑ Guyot M-C, Hantraye P, Dolan R, Palfi S, Maziere M, Brouillet E.Quantifiable bradykinesia, gait abnormalities and Huntington’s disease-like striatal lesions in rats chronically treated with 3-nitropropionic acid. Neuroscience. 1997;79(1):45–56.
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