2cf5

From Proteopedia

(Difference between revisions)
Jump to: navigation, search

OCA (Talk | contribs)
(New page: 200px<br /> <applet load="2cf5" size="450" color="white" frame="true" align="right" spinBox="true" caption="2cf5, resolution 2.0&Aring;" /> '''CRYSTAL STRUCTURES O...)
Next diff →

Revision as of 14:19, 29 October 2007

Image:2cf5.gif

2cf5, resolution 2.0Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURES OF THE ARABIDOPSIS CINNAMYL ALCOHOL DEHYDROGENASES, ATCAD5

Overview

The cinnamyl alcohol dehydrogenase (CAD) multigene family in planta, encodes proteins catalyzing the reductions of various phenylpropenyl, aldehyde derivatives in a substrate versatile manner, and whose metabolic, products are the precursors of structural lignins, health-related lignans, and various other metabolites. In Arabidopsis thaliana, the two isoforms, AtCAD5 and AtCAD4, are the catalytically most active being viewed as, mainly involved in the formation of guaiacyl/syringyl lignins. In this, study, we determined the crystal structures of AtCAD5 in the apo-form and, as a binary complex with NADP+, respectively, and modeled that of AtCAD4., Both AtCAD5 and AtCAD4 are dimers with two zinc ions per subunit and, belong to the Zn-dependent medium chain dehydrogenase/reductase (MDR), ... [(full description)]

About this Structure

2CF5 is a [Single protein] structure of sequence from [Arabidopsis thaliana] with ZN as [ligand]. Active as [[1]], with EC number [1.1.1.195]. Full crystallographic information is available from [OCA].

Reference

Crystal structures and catalytic mechanism of the Arabidopsis cinnamyl alcohol dehydrogenases AtCAD5 and AtCAD4., Youn B, Camacho R, Moinuddin SG, Lee C, Davin LB, Lewis NG, Kang C, Org Biomol Chem. 2006 May 7;4(9):1687-97. Epub 2006 Apr 4. PMID:16633561

Page seeded by OCA on Mon Oct 29 16:23:52 2007

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2cf5"
Personal tools