From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1w1q.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1w1q.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1w1q| PDB=1w1q | SCENE= }} | | {{STRUCTURE_1w1q| PDB=1w1q | SCENE= }} |
| | | | |
| - | '''PLANT CYTOKININ DEHYDROGENASE IN COMPLEX WITH ISOPENTENYLADENINE'''
| + | ===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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15321719}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15321719 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_15321719}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 30: |
Line 34: |
| | [[Category: Flavoprotein]] | | [[Category: Flavoprotein]] |
| | [[Category: Oxidoreductase]] | | [[Category: Oxidoreductase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:01:50 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:52:36 2008'' |
Revision as of 14:52, 27 July 2008
Template:STRUCTURE 1w1q
PLANT CYTOKININ DEHYDROGENASE IN COMPLEX WITH ISOPENTENYLADENINE
Template:ABSTRACT PUBMED 15321719
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
Page seeded by OCA on Sun Jul 27 17:52:36 2008
