1r37

From Proteopedia

Revision as of 23:07, 20 November 2007

Alcohol dehydrogenase from sulfolobus solfataricus complexed with NAD(H) and 2-ethoxyethanol

Overview

The crystal structure of a ternary complex of the alcohol dehydrogenase, from the archaeon Sulfolobus solfataricus (SsADH) has been determined at, 2.3 A. The asymmetric unit contains a dimer with a NADH and a, 2-ethoxyethanol molecule bound to each subunit. The comparison with the, apo structure of the enzyme reveals that this medium chain ADH undergoes a, substantial conformational change in the apo-holo transition, accompanied, by loop movements at the domain interface. The extent of domain closure is, similar to that observed for the classical horse liver ADH, although some, differences are found which can be related to the different oligomeric, states of the enzymes. Compared to its apo form, the SsADH ternary complex, shows a change in the ligation state of the active site zinc ion which is, no longer bound to Glu69, providing additional evidence of the dynamic, role played by the conserved glutamate residue in ADHs. In addition, the, structure presented here allows the identification of the substrate site, and hence of the residues that are important in the binding of both the, substrate and the coenzyme.

About this Structure

1R37 is a Single protein structure of sequence from Sulfolobus solfataricus with ZN, NAD and ETX as ligands. Active as Alcohol dehydrogenase, with EC number 1.1.1.1 Full crystallographic information is available from OCA.

Reference

Crystal structure of a ternary complex of the alcohol dehydrogenase from Sulfolobus solfataricus., Esposito L, Bruno I, Sica F, Raia CA, Giordano A, Rossi M, Mazzarella L, Zagari A, Biochemistry. 2003 Dec 16;42(49):14397-407. PMID:14661950

Page seeded by OCA on Wed Nov 21 01:14:19 2007