Direct observation of correlated interdomain motion in alcohol dehydrogenase.
Interdomain motions in proteins are essential to enable or promote biochemical function. Neutron spin-echo spectroscopy is used to directly observe the domain dynamics of the protein alcohol dehydrogenase. The collective motion of domains as revealed by their coherent form factor relates to the cleft opening dynamics between the binding and the catalytic domains enabling binding and release of the functional important cofactor. The cleft opening mode hardens as a result of an overall stiffening of the domain complex due to the binding of the cofactor.
Institut für Festkörperforschung, Forschungszentrum Jülich, D-52425 Jülich, Germany.
Ralf
R
Biehl
Bernd
B
Hoffmann
Michael
M
Monkenbusch
Peter
P
Falus
Sylvain
S
Préost
Rudolf
R
Merkel
Dieter
D
Richter
D000426:Alcohol Dehydrogenase / Q000737:chemistry* / Q000378:metabolism; D008956:Models, Chemical; D008958:Models, Molecular; D009243:NAD / Q000737:chemistry / Q000378:metabolism; D017434:Protein Structure, Tertiary; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000378:metabolism; D013696:Temperature; D013816:Thermodynamics
D029701:Saccharomyces cerevisiae Proteins; D009243:NAD; D000426:Alcohol Dehydrogenase