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===='''FAD cofactor binding domain'''====
===='''FAD cofactor binding domain'''====
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The FAD cofactor has a covalent way of binding with the enzyme. The attachment takes place at the <scene name='68/686754/His105/1'>His105</scene> in the GHS domain of the enzyme. The one binds the 8-methyl group of the flavin ring (isoalloxazine ring). <scene name='41/413140/His105_and_fad/1'>TextToBeDisplayed</scene>
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The FAD cofactor has a covalent way of binding with the enzyme. The attachment takes place at the His105 in the GHS domain of the enzyme. The one binds the <scene name='41/413140/His105_and_fad/1'> 8-methyl group of the flavin ring</scene> (isoalloxazine ring).
The two negative charges brought by the pyrophosphate of the FAD cofactor is compensated by the nitrogen atoms of a few amino acids such as <scene name='68/686754/Pyrophosphate_aa/1'>Gly102, Arg103, Gly104, His105, Ser106 and Thr174</scene>.
The two negative charges brought by the pyrophosphate of the FAD cofactor is compensated by the nitrogen atoms of a few amino acids such as <scene name='68/686754/Pyrophosphate_aa/1'>Gly102, Arg103, Gly104, His105, Ser106 and Thr174</scene>.

Revision as of 15:00, 9 January 2015

2qkn

Crystal structure of Maize cytokinin oxidase/dehydrogenase complexed with phenylurea inhibitor CPPU

2qkn, resolution 2.15Å

Drag the structure with the mouse to rotate

References

  1. 1.0 1.1 1.2 1.3 1.4 Frebortova J, Novak O, Frebort I, Jorda R. Degradation of cytokinins by maize cytokinin dehydrogenase is mediated by free radicals generated by enzymatic oxidation of natural benzoxazinones. Plant J. 2010 Feb 1;61(3):467-81. doi: 10.1111/j.1365-313X.2009.04071.x. Epub, 2009 Nov 14. PMID:19912568 doi:http://dx.doi.org/10.1111/j.1365-313X.2009.04071.x
  2. 2.0 2.1 2.2 2.3 2.4 2.5 2.6 Kopecny D, Briozzo P, Popelkova H, Sebela M, Koncitikova R, Spichal L, Nisler J, Madzak C, Frebort I, Laloue M, Houba-Herin N. Phenyl- and benzylurea cytokinins as competitive inhibitors of cytokinin oxidase/dehydrogenase: a structural study. Biochimie. 2010 Aug;92(8):1052-62. Epub 2010 May 15. PMID:20478354 doi:10.1016/j.biochi.2010.05.006
  3. Kopecny D, Sebela M, Briozzo P, Spichal L, Houba-Herin N, Masek V, Joly N, Madzak C, Anzenbacher P, Laloue M. Mechanism-based inhibitors of cytokinin oxidase/dehydrogenase attack FAD cofactor. J Mol Biol. 2008 Jul 25;380(5):886-99. Epub 2008 May 24. PMID:18571199 doi:10.1016/j.jmb.2008.05.044
  4. 4.0 4.1 4.2 4.3 Kopecny D, Pethe C, Sebela M, Houba-Herin N, Madzak C, Majira A, Laloue M. High-level expression and characterization of Zea mays cytokinin oxidase/dehydrogenase in Yarrowia lipolytica. Biochimie. 2005 Nov;87(11):1011-22. PMID:15927342 doi:http://dx.doi.org/10.1016/j.biochi.2005.04.006
  5. 5.0 5.1 5.2 5.3 5.4 Malito E, Coda A, Bilyeu KD, Fraaije MW, Mattevi A. Structures of Michaelis and product complexes of plant cytokinin dehydrogenase: implications for flavoenzyme catalysis. J Mol Biol. 2004 Aug 27;341(5):1237-49. PMID:15321719 doi:http://dx.doi.org/10.1016/j.jmb.2004.06.083
  6. 6.0 6.1 Schmulling T, Werner T, Riefler M, Krupkova E, Bartrina y Manns I. Structure and function of cytokinin oxidase/dehydrogenase genes of maize, rice, Arabidopsis and other species. J Plant Res. 2003 Jun;116(3):241-52. Epub 2003 Apr 29. PMID:12721786 doi:http://dx.doi.org/10.1007/s10265-003-0096-4

Proteopedia Page Contributors and Editors (what is this?)

Pauline Hanns, Léo Alcapia

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