2cf5

From Proteopedia

(Difference between revisions)

Revision as of 07:38, 11 March 2020

Crystal Structures of the Arabidopsis Cinnamyl Alcohol Dehydrogenases, AtCAD5

Structural highlights

2cf5 is a 1 chain structure with sequence from Arath. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	2cf6
Activity:	Cinnamyl-alcohol dehydrogenase, with EC number 1.1.1.195
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CADH2_ARATH] Involved in lignin biosynthesis. Catalyzes the final step specific for the production of lignin monomers. Catalyzes the NADPH-dependent reduction of coniferaldehyde, 5-hydroxyconiferaldehyde, sinapaldehyde, 4-coumaraldehyde and caffeyl aldehyde to their respective alcohols.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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) superfamily, on the basis of their overall 2-domain structures and distribution of secondary structural elements. The catalytic Zn2+ ions in both enzymes are tetrahedrally coordinated, but differ from those in horse liver alcohol dehydrogenase since the carboxyl side-chain of Glu70 is ligated to Zn2+ instead of water. Using AtCAD5, site-directed mutagenesis of Glu70 to alanine resulted in loss of catalytic activity, thereby indicating that perturbation of the Zn2+ coordination was sufficient to abolish catalytic activity. The substrate-binding pockets of both AtCAD5 and AtCAD4 were also examined, and found to be significantly different and smaller compared to that of a putative aspen sinapyl alcohol dehydrogenase (SAD) and a putative yeast CAD. While the physiological roles of the aspen SAD and the yeast CAD are uncertain, they nevertheless have a high similarity in the overall 3D structures to AtCAD5 and 4. With the bona fide CAD's from various species, nine out of the twelve residues which constitute the proposed substrate-binding pocket were, however, conserved. This is provisionally considered as indicative of a characteristic fingerprint for the CAD family.

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Kim SJ, Kim MR, Bedgar DL, Moinuddin SG, Cardenas CL, Davin LB, Kang C, Lewis NG. Functional reclassification of the putative cinnamyl alcohol dehydrogenase multigene family in Arabidopsis. Proc Natl Acad Sci U S A. 2004 Feb 10;101(6):1455-60. Epub 2004 Jan 26. PMID:14745009 doi:http://dx.doi.org/10.1073/pnas.0307987100
↑ Youn B, Camacho R, Moinuddin SG, Lee C, Davin LB, Lewis NG, Kang C. Crystal structures and catalytic mechanism of the Arabidopsis cinnamyl alcohol dehydrogenases AtCAD5 and AtCAD4. Org Biomol Chem. 2006 May 7;4(9):1687-97. Epub 2006 Apr 4. PMID:16633561 doi:10.1039/b601672c

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
-==CRYSTAL STRUCTURES OF THE ARABIDOPSIS CINNAMYL ALCOHOL DEHYDROGENASES, ATCAD5==
-<StructureSection load='2cf5' size='340' side='right' caption='[[2cf5]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+==Crystal Structures of the Arabidopsis Cinnamyl Alcohol Dehydrogenases, AtCAD5==
+<StructureSection load='2cf5' size='340' side='right'caption='[[2cf5]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[2cf5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CF5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CF5 FirstGlance]. <br>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2cf6|2cf6]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cinnamyl-alcohol_dehydrogenase Cinnamyl-alcohol dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.195 1.1.1.195] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cf5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cf5 OCA], [http://pdbe.org/2cf5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cf5 RCSB], [http://www.ebi.ac.uk/pdbsum/2cf5 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cf5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cf5 OCA], [http://pdbe.org/2cf5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cf5 RCSB], [http://www.ebi.ac.uk/pdbsum/2cf5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2cf5 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cf/2cf5_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cf/2cf5_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 31: / Line 32: @@
 ==See Also==
-*[[Alcohol dehydrogenase|Alcohol dehydrogenase]]
+*[[Acetylcholinesterase 3D structures|Acetylcholinesterase 3D structures]]
-*[[3D structures of acetylcholinesterase|3D structures of acetylcholinesterase]]
+*[[Alcohol dehydrogenase 3D structures|Alcohol dehydrogenase 3D structures]]
 == References ==
 <references/>
@@ Line 39: / Line 40: @@
 [[Category: Arath]]
 [[Category: Cinnamyl-alcohol dehydrogenase]]
+[[Category: Large Structures]]
 [[Category: Camacho, R]]
 [[Category: Davin, L B]]
@@ Line 50: / Line 52: @@
 [[Category: Nadp]]
 [[Category: Oxidoreductase]]
+[[Category: Zinc]]

2cf5

From Proteopedia

Revision as of 07:38, 11 March 2020

Crystal Structures of the Arabidopsis Cinnamyl Alcohol Dehydrogenases, AtCAD5

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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