Crystal Structure Analysis of Coniferyl Alcohol 9-O-Methyltransferase from Linum Nodiflorum in Complex with Coniferyl Alcohol 9-Methyl Ether and S -Adenosyl-L-Homocysteine

Structural analysis of coniferyl alcohol 9-O-methyltransferase from Linum nodiflorum reveals a novel active-site environment.

S-adenosyl-L-methionine-dependent coniferyl alcohol 9-O-methyltransferase

MGSSHHHHHHSSGLVPRGSHMDAATAVELLDAQPQVWHHFLGYINSMTLQCALELDIADVIHRHGHPIPLNQLAAALEIP
QTKAPFLSRLMRMLVHLGYFTQVITKPEDENDDVLPSYWLAPLSRLLLKQNPYNARSLTFCSVHEHLVDPWRQMSAWLRT
GKEDGKDTPNAFAFAHEGKKVYEVCSEDANFSQLFSEGMAGDSWLFSRALVSKCRDAFEGLSSLVDVGGGTGNTSKVIAE
TFPNIHCTVFDLPHVVSGPKQTHPNLDYESGNMFTDEIPHADAVLFKWVLCDWPDEPVLKMLKQCKKALTKNGVKGKLMI
ADHVLDHESCNDSNSMGTSLILDMLFMSFLEGSLRTEKQWAKLFAEAGFKDYKITPVGGLRVLIEVYP

1 M Na/K phosphate, 0,7M ammonium sulfate, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K

The same protein complexed with coniferyl alcohol

Rossmann fold, Dimer, small molecule O-methyltransferase, TRANSFERASE, S-Adenosyl-L-methionine, coniferyl alcohol, S -Adenosyl-L-homocysteine

MDAATAVELLDAQPQVWHHFLGYINSMTLQCALELDIADVIHRHGHPIPLNQLAAALEIPQTKAPFLSRLMRMLVHLGYF
TQVITKPEDENDDVLPSYWLAPLSRLLLKQNPYNARSLTFCSVHEHLVDPWRQMSAWLRTGKEDGKDTPNAFAFAHEGKK
VYEVCSEDANFSQLFSEGMAGDSWLFSRALVSKCRDAFEGLSSLVDVGGGTGNTSKVIAETFPNIHCTVFDLPHVVSGPK
QTHPNLDYESGNMFTDEIPHADAVLFKWVLCDWPDEPVLKMLKQCKKALTKNGVKGKLMIADHVLDHESCNDSNSMGTSL
ILDMLFMSFLEGSLRTEKQWAKLFAEAGFKDYKITPVGGLRVLIEVYP