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1w1q

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[[Category: oxidoreductase]]
[[Category: oxidoreductase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:55:46 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 16:21:59 2007''

Revision as of 14:17, 30 October 2007


1w1q, resolution 1.80Å

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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 [Cytokinin dehydrogenase], with EC number [1.5.99.12]. Structure known Active Site: AC1. 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

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