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2cf6

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Crystal Structures of the Arabidopsis Cinnamyl Alcohol Dehydrogenases AtCAD5

Structural highlights

2cf6 is a 1 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.6Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CADH5_ARATH Involved in lignin biosynthesis in the floral stem. 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] ^[2] ^[3]

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^[4]

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

References

↑ Sibout R, Eudes A, Pollet B, Goujon T, Mila I, Granier F, Séguin A, Lapierre C, Jouanin L. Expression pattern of two paralogs encoding cinnamyl alcohol dehydrogenases in Arabidopsis. Isolation and characterization of the corresponding mutants. Plant Physiol. 2003 Jun;132(2):848-60. PMID:12805615 doi:10.1104/pp.103.021048
↑ 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
↑ Sibout R, Eudes A, Mouille G, Pollet B, Lapierre C, Jouanin L, Séguin A. CINNAMYL ALCOHOL DEHYDROGENASE-C and -D are the primary genes involved in lignin biosynthesis in the floral stem of Arabidopsis. Plant Cell. 2005 Jul;17(7):2059-76. PMID:15937231 doi:10.1105/tpc.105.030767
↑ 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/2cf6"

@@ Line 3: / Line 3: @@
 <StructureSection load='2cf6' size='340' side='right'caption='[[2cf6]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2cf6]] 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=2CF6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CF6 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2cf6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CF6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CF6 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2cf5|2cf5]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=2cf6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cf6 OCA], [https://pdbe.org/2cf6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cf6 RCSB], [https://www.ebi.ac.uk/pdbsum/2cf6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cf6 ProSAT]</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=2cf6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cf6 OCA], [http://pdbe.org/2cf6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cf6 RCSB], [http://www.ebi.ac.uk/pdbsum/2cf6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2cf6 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CADH2_ARATH 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.<ref>PMID:14745009</ref>
+[https://www.uniprot.org/uniprot/CADH5_ARATH CADH5_ARATH] Involved in lignin biosynthesis in the floral stem. 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.<ref>PMID:12805615</ref> <ref>PMID:14745009</ref> <ref>PMID:15937231</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 37: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Arath]]
+[[Category: Arabidopsis thaliana]]
-[[Category: Cinnamyl-alcohol dehydrogenase]]
 [[Category: Large Structures]]
-[[Category: Camacho, R]]
+[[Category: Camacho R]]
-[[Category: Davin, L B]]
+[[Category: Davin LB]]
-[[Category: Kang, C]]
+[[Category: Kang C]]
-[[Category: Lee, C]]
+[[Category: Lee C]]
-[[Category: Lewis, N G]]
+[[Category: Lewis NG]]
-[[Category: Moinuddin, S G]]
+[[Category: Moinuddin SG]]
-[[Category: Youn, B]]
+[[Category: Youn B]]
-[[Category: Lignin biosynthesis]]
-[[Category: Metal-binding]]
-[[Category: Nadp]]
-[[Category: Oxidoreductase]]
-[[Category: Zinc]]

2cf6

From Proteopedia

Current revision

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?)

Views

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