Structure of the complex of active site metal-depleted horse liver alcohol dehydrogenase and NADH.
AUTOR(ES)
Schneider, G
RESUMO
The complex between active site-specific metal-depleted horse liver alcohol dehydrogenase and NADH has been studied with X-ray crystallographic methods to 2.9 A resolution. The electron density maps revealed that only the catalytic zinc ions are removed, whereas the non-catalytic zinc sites ae fully occupied. A gross conformational change in the protein induced by co-enzyme binding takes place in this enzyme species despite the absence of the metal ion in the catalytic center. This circumstance is of great importance in the understanding and further analysis of the trigger mechanisms operating during the conformation transition in alcohol dehydrogenase, since the catalytic center is located at the hinge region for a domain rotation in the subunit, and the metal atom is essential for catalysis. The overall protein structure is the same as that of an NADH complex of the native zinc enzyme and the co-enzyme is bound in a similar manner. The local structural changes observed are restricted to the empty metal binding site.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=555170Documentos Relacionados
- Crystal structures of the active site in specifically metal-depleted and cobalt-substituted horse liver alcohol dehydrogenase derivatives.
- Coordination environment of the active-site metal ion of liver alcohol dehydrogenase.
- Nanosecond time-resolved circular polarization of fluorescence: study of NADH bound to horse liver alcohol dehydrogenase.
- Structural and functional zinc in horse liver alcohol dehydrogenase.
- Ten-nanosecond molecular dynamics simulation of the motions of the horse liver alcohol dehydrogenase⋅PhCH2O− complex