1yqd
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1yqd |SIZE=350|CAPTION= <scene name='initialview01'>1yqd</scene>, resolution 1.65Å | |PDB= 1yqd |SIZE=350|CAPTION= <scene name='initialview01'>1yqd</scene>, resolution 1.65Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <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> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yqd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yqd OCA], [http://www.ebi.ac.uk/pdbsum/1yqd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1yqd RCSB]</span> | ||
}} | }} | ||
| Line 25: | Line 28: | ||
[[Category: Bomati, E K.]] | [[Category: Bomati, E K.]] | ||
[[Category: Noel, J P.]] | [[Category: Noel, J P.]] | ||
| - | [[Category: DTT]] | ||
| - | [[Category: GOL]] | ||
| - | [[Category: NAP]] | ||
| - | [[Category: ZN]] | ||
[[Category: biosynthesis]] | [[Category: biosynthesis]] | ||
[[Category: lignin]] | [[Category: lignin]] | ||
| Line 38: | Line 37: | ||
[[Category: zinc-dependent]] | [[Category: zinc-dependent]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:17:52 2008'' |
Revision as of 22:17, 30 March 2008
| |||||||
| , resolution 1.65Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Activity: | Cinnamyl-alcohol dehydrogenase, with EC number 1.1.1.195 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Sinapyl Alcohol Dehydrogenase complexed with NADP+
Overview
We describe the three-dimensional structure of sinapyl alcohol dehydrogenase (SAD) from Populus tremuloides (aspen), a member of the NADP(H)-dependent dehydrogenase family that catalyzes the last reductive step in the formation of monolignols. The active site topology revealed by the crystal structure substantiates kinetic results indicating that SAD maintains highest specificity for the substrate sinapaldehyde. We also report substantial substrate inhibition kinetics for the SAD-catalyzed reduction of hydroxycinnamaldehydes. Although SAD and classical cinnamyl alcohol dehydrogenases (CADs) catalyze the same reaction and share some sequence identity, the active site topology of SAD is strikingly different from that predicted for classical CADs. Kinetic analyses of wild-type SAD and several active site mutants demonstrate the complexity of defining determinants of substrate specificity in these enzymes. These results, along with a phylogenetic analysis, support the inclusion of SAD in a plant alcohol dehydrogenase subfamily that includes cinnamaldehyde and benzaldehyde dehydrogenases. We used the SAD three-dimensional structure to model several of these SAD-like enzymes, and although their active site topologies largely mirror that of SAD, we describe a correlation between substrate specificity and amino acid substitution patterns in their active sites. The SAD structure thus provides a framework for understanding substrate specificity in this family of enzymes and for engineering new enzyme specificities.
About this Structure
1YQD is a Single protein structure of sequence from Populus tremuloides. Full crystallographic information is available from OCA.
Reference
Structural and kinetic basis for substrate selectivity in Populus tremuloides sinapyl alcohol dehydrogenase., Bomati EK, Noel JP, Plant Cell. 2005 May;17(5):1598-611. Epub 2005 Apr 13. PMID:15829607
Page seeded by OCA on Mon Mar 31 01:17:52 2008
