A model of photoprobe docking with beta1,4-galactosyltransferase identifies a possible carboxylate involved in glycosylation steps.
A molecular docking study has been performed on the interaction of beta1,4-galactosyltransferase with an acceptor site photoprobe. This is based on an acceptor site peptide fragment which was recently identified by the use of a photoprobe. The present model strongly suggests that the carboxylate group of Asp318 could be involved in the activation of the acceptor sugar 4-OH for the efficient galactosyltransfer. The result also exemplified that the combination of photoaffinity labeling with crystallography is a powerful method for the detailed structural analysis of ligand protein complex.
Hatanaka
Y
Y
Faculty of Pharmaceutical Sciences, Toyama Medical and Pharmaceutical University, Japan. yasu@ms.toyama-mpu.ac.jp
Ishiguro
M
M
Hashimoto
M
M
Gastinel
L N
LN
Nakagomi
K
K
D001224:Aspartic Acid / Q000378:metabolism; D019921:Biotinylation; D020134:Catalytic Domain; D003978:Diazomethane / Q000737:chemistry; D005700:Galactosyltransferases / Q000737:chemistry* / Q000378:metabolism; D006031:Glycosylation; D008956:Models, Chemical; D008958:Models, Molecular; D015335:Molecular Probes; D019920:Photoaffinity Labels / Q000378:metabolism*
D015335:Molecular Probes; D019920:Photoaffinity Labels; D001224:Aspartic Acid; D003978:Diazomethane; D005700:Galactosyltransferases; C119701:beta-1,4-galactosyltransferase I