From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1kyw.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1kyw.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1kyw| PDB=1kyw | SCENE= }} | | {{STRUCTURE_1kyw| PDB=1kyw | SCENE= }} |
| | | | |
| - | '''Crystal Structure Analysis of Caffeic Acid/5-hydroxyferulic acid 3/5-O-methyltransferase in complex with 5-hydroxyconiferaldehyde'''
| + | ===Crystal Structure Analysis of Caffeic Acid/5-hydroxyferulic acid 3/5-O-methyltransferase in complex with 5-hydroxyconiferaldehyde=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | Caffeic acid/5-hydroxyferulic acid 3/5-O-methyltransferase (COMT) from alfalfa is an S-adenosyl-L-Met-dependent O-methyltransferase involved in lignin biosynthesis. COMT methylates caffeoyl- and 5-hydroxyferuloyl-containing acids, aldehydes, and alcohols in vitro while displaying a kinetic preference for the alcohols and aldehydes over the free acids. The 2.2-A crystal structure of COMT in complex with S-adenosyl-L-homocysteine (SAH) and ferulic acid (ferulate form), as well as the 2.4-A crystal structure of COMT in complex with SAH and 5-hydroxyconiferaldehyde, provide a structural understanding of the observed substrate preferences. These crystal structures identify residues lining the active site surface that contact the substrates. Structurally guided site-directed mutagenesis of active site residues was performed with the goal of altering the kinetic preferences for physiological substrates. The kinetic parameters of the COMT mutants versus wild-type enzyme are presented, and coupled with the high-resolution crystal structures, they will serve as a starting point for the in vivo manipulation of lignin monomers in transgenic plants. Ultimately, this structurally based approach to metabolic engineering will allow the further alteration of the lignin biosynthetic pathway in agronomically important plants. This approach will lead to a better understanding of the in vivo operation of the potential metabolic grid for monolignol biosynthesis.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_12084826}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12084826 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_12084826}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 31: |
Line 35: |
| | [[Category: O-methyltransferase]] | | [[Category: O-methyltransferase]] |
| | [[Category: Protein-ligand complex]] | | [[Category: Protein-ligand complex]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:20:29 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 11:19:15 2008'' |
Revision as of 08:19, 2 July 2008
Template:STRUCTURE 1kyw
Crystal Structure Analysis of Caffeic Acid/5-hydroxyferulic acid 3/5-O-methyltransferase in complex with 5-hydroxyconiferaldehyde
Template:ABSTRACT PUBMED 12084826
About this Structure
1KYW is a Single protein structure of sequence from Medicago sativa. Full crystallographic information is available from OCA.
Reference
Structural basis for the modulation of lignin monomer methylation by caffeic acid/5-hydroxyferulic acid 3/5-O-methyltransferase., Zubieta C, Kota P, Ferrer JL, Dixon RA, Noel JP, Plant Cell. 2002 Jun;14(6):1265-77. PMID:12084826
Page seeded by OCA on Wed Jul 2 11:19:15 2008
