1w1q

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[[Image:1w1q.gif|left|200px]]<br /><applet load="1w1q" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1w1q.gif|left|200px]]
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caption="1w1q, resolution 1.80&Aring;" />
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'''PLANT CYTOKININ DEHYDROGENASE IN COMPLEX WITH ISOPENTENYLADENINE'''<br />
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{{Structure
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|PDB= 1w1q |SIZE=350|CAPTION= <scene name='initialview01'>1w1q</scene>, resolution 1.80&Aring;
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|SITE= <scene name='pdbsite=AC1:Nag+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene> and <scene name='pdbligand=ZIP:N-(3-METHYLBUT-2-EN-1-YL)-9H-PURIN-6-AMINE'>ZIP</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Cytokinin_dehydrogenase Cytokinin dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.99.12 1.5.99.12]
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|GENE=
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}}
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'''PLANT CYTOKININ DEHYDROGENASE IN COMPLEX WITH ISOPENTENYLADENINE'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1W1Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Zea_mays Zea mays] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=FAD:'>FAD</scene> and <scene name='pdbligand=ZIP:'>ZIP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Cytokinin_dehydrogenase Cytokinin dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.99.12 1.5.99.12] Known structural/functional Site: <scene name='pdbsite=AC1:Nag+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W1Q OCA].
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1W1Q is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Zea_mays Zea mays]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W1Q OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15321719 15321719]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15321719 15321719]
[[Category: Cytokinin dehydrogenase]]
[[Category: Cytokinin dehydrogenase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: oxidoreductase]]
[[Category: oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:39:32 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:50:51 2008''

Revision as of 12:50, 20 March 2008

Image:1w1q.gif


PDB ID 1w1q

Drag the structure with the mouse to rotate
, resolution 1.80Å
Sites:
Ligands: , and
Activity: Cytokinin dehydrogenase, with EC number 1.5.99.12
Coordinates: save as pdb, mmCIF, xml



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 the structural analysis of the complexes with a slowly reacting substrate and the reaction product, which correspond to the states immediately before (Michaelis complex) and after (product complex) oxidation has taken place. The substrate displays a "plug-into-socket" binding mode that seals the catalytic site and precisely positions the carbon atom undergoing oxidation in close contact with the reactive locus of the flavin. A polarising H-bond between the substrate amine group and an Asp-Glu pair may facilitate oxidation. Substrate to product conversion results in small atomic movements, which lead to a planar conformation of the reaction product allowing double-bond conjugation. These features in the mechanism of amine recognition and oxidation differ from those observed in other flavin-dependent amine oxidases.

About this Structure

1W1Q is a Single protein structure of sequence from Zea mays. 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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