1w1q
From Proteopedia
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(New page: 200px<br /> <applet load="1w1q" size="450" color="white" frame="true" align="right" spinBox="true" caption="1w1q, resolution 1.80Å" /> '''PLANT CYTOKININ DEH...)
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Revision as of 17:51, 29 October 2007
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PLANT CYTOKININ DEHYDROGENASE IN COMPLEX WITH ISOPENTENYLADENINE
Overview
Cytokinins form a diverse class of compounds that are essential for plant, growth. Cytokinin dehydrogenase has a major role in the control of the, levels of these plant hormones by catalysing their irreversible oxidation., The crystal structure of Zea mays cytokinin dehydrogenase displays the, same two-domain topology of the flavoenzymes of the vanillyl-alcohol, oxidase family but its active site cannot be related to that of any other, family member. The X-ray analysis reveals a bipartite architecture of the, catalytic centre, which consists of a funnel-shaped region on the protein, surface and an internal cavity lined by the flavin ring. A pore with, diameter of about 4A connects the two active-site regions. Snapshots of, two critical steps along the reaction cycle were obtained through ... [(full description)]
About this Structure
1W1Q is a [Single protein] structure of sequence from [Zea mays] with NAG, FAD and ZIP as [ligands]. Active as [[1]], with EC number [1.5.99.12]. Full crystallographic information is available from [OCA].
Reference
Structures of Michaelis and product complexes of plant cytokinin dehydrogenase: implications for flavoenzyme catalysis., Malito E, Coda A, Bilyeu KD, Fraaije MW, Mattevi A, J Mol Biol. 2004 Aug 27;341(5):1237-49. PMID:15321719
Page seeded by OCA on Mon Oct 29 19:56:12 2007
Categories: Single protein | Zea mays | Malito, E. | Mattevi, A. | FAD | NAG | ZIP | Cytokinin | Fad | Flavin | Flavoprotein | Oxidoreductase