Sandbox GGC1

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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 are eight parallel beta pleaded strands that are depicted in pink surrounded by eight alpha helixes in blue.<ref>Crystal structure of yeast nitronate monooxygenase from <i>Cyberlindnera saturnus</i>Agniswamy J Reis R Wang Y et. al. Proteins: Structure, Function, and Bioinformatics, 2018</ref>
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 are eight parallel beta pleaded strands that are depicted in pink surrounded by eight alpha helixes in blue.<ref>Crystal structure of yeast nitronate monooxygenase from <i>Cyberlindnera saturnus</i>Agniswamy J Reis R Wang Y et. al. Proteins: Structure, Function, and Bioinformatics, 2018</ref>
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The N- and C- termini
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The active site is located in an area formed by the FMN-binding domain and the substrate-binding domain. Residues that surround the active site and form a ring around FMN consist of M23, A24, F79, Y119, H147, H197, Y321, Y325, and L348. <scene name='75/752263/Active_site_fmn/1'>The active site is depicted with the surrounding residues that form a ring around FMN.</scene>
FMN Binding site is formed with hydrogen bonds with main chain amino acids of G240, G261, and T262. <ref>Crystal structure of yeast nitronate monooxygenase from <i>Cyberlindnera saturnus</i>
FMN Binding site is formed with hydrogen bonds with main chain amino acids of G240, G261, and T262. <ref>Crystal structure of yeast nitronate monooxygenase from <i>Cyberlindnera saturnus</i>
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Agniswamy J Reis R Wang Y et. al. Proteins: Structure, Function, and Bioinformatics, 2018</ref> <scene name='75/752263/Fmn_binding_site/3'> This is a view of the FMN Binding site with labeled amino acid residues.</scene>
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Agniswamy J Reis R Wang Y et. al. Proteins: Structure, Function, and Bioinformatics, 2018</ref> <scene name='75/752263/Fmn_binding_site/3'> This is a view of the FMN Binding site with labeled amino acid residues.</scene> Also, the phosphate group of FMN forms a hydrogen bond with the side-chain hydroxyl group of T262.
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The phosphate group of FMN forms a hydrogen bond with the side-chain hydroxyl group of T262.
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</StructureSection>
</StructureSection>
== References ==
== References ==
<references/>
<references/>

Revision as of 23:48, 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.
  10. ↑ Crystal structure of yeast nitronate monooxygenase from Cyberlindnera saturnusAgniswamy J Reis R Wang Y et. al. Proteins: Structure, Function, and Bioinformatics, 2018
  11. ↑ Crystal structure of yeast nitronate monooxygenase from Cyberlindnera saturnus Agniswamy J Reis R Wang Y et. al. Proteins: Structure, Function, and Bioinformatics, 2018
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