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Ribbon type representation of the tetramer of
T. brockii alcohol dehydrogenase

Image 3

[From: Y. Korkhin, A. J. Kalb (Gilboa), M. Peretz, O. Bogin, Y. Burstein, and F. Frolow,
"NADP-dependent Bacterial Alcohol Dehydrogenases: Crystal Structure, Cofactor-binding and
Cofactor Specificity of the ADHs of Clostridium beijerinckii and Thermoanaerobacter brockii"
J. Mol. Biol. 278, 967-981 (1998).]

Our results indicated that TBADH and its mesophilic counterparts, CBADH, EHADH, EIADH, and MPADH, would provide an excellent and reliable model system for studying the molecular basis of enzyme thermostability.

To this end, the respective crystal structures of holo- and apo-CBADH were determined at 2.05 Angstrom; and 2.15 Angstrom; resolution, and that of holo-TBADH at 2.5 Angstrom; resolution (in collaboration with Dr. Felix Frolow).

The 3-D structures of these proteins were the first to be determined for a prokaryotic ADH, as well as for an NADP(H)-dependent ADH. CBADH and TBADH have very similar three-dimensional structures. The monomers are composed of two domains: a cofactor-binding domain and a catalytic domain.

This file was last modified on Monday, 25-Dec-2000 16:48:29 IST.

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