1llu
From Proteopedia
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THE TERNARY COMPLEX OF PSEUDOMONAS AERUGINOSA ALCOHOL DEHYDROGENASE WITH ITS COENZYME AND WEAK SUBSTRATE
Overview
Pseudomonas aeruginosa alcohol dehydrogenase (PaADH; ADH, EC 1.1.1.1), catalyzes the reversible oxidation of primary and secondary alcohols to, the corresponding aldehydes and ketones, using NAD as coenzyme. We, crystallized the ternary complex of PaADH with its coenzyme and a, substrate molecule and determined its structure at a resolution of 2.3 A, using the molecular replacement method. The PaADH tetramer comprises four, identical chains of 342 amino acid residues each and obeys ~222-point, symmetry. The PaADH monomer is structurally similar to alcohol, dehydrogenase monomers from vertebrates, archaea, and bacteria. The, stabilization of the ternary complex of PaADH, the coenzyme, and the poor, substrate ethylene glycol (k(cat) = 4.5 sec(-1); Km > 200 mM) was due to, the blocked exit of the coenzyme in the crystalline state, combined with a, high (2.5 M) concentration of the substrate. The structure of the ternary, complex presents the precise geometry of the Zn coordination complex, the, proton-shuttling system, and the hydride transfer path. The ternary, complex structure also suggests that the low efficiency of ethylene glycol, as a substrate results from the presence of a second hydroxyl group in, this molecule.
About this Structure
1LLU is a Single protein structure of sequence from Pseudomonas aeruginosa with ZN, NAD and EDO as ligands. Active as Alcohol dehydrogenase, with EC number 1.1.1.1 Full crystallographic information is available from OCA.
Reference
The ternary complex of Pseudomonas aeruginosa alcohol dehydrogenase with NADH and ethylene glycol., Levin I, Meiri G, Peretz M, Burstein Y, Frolow F, Protein Sci. 2004 Jun;13(6):1547-56. PMID:15152088
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