1R37

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

Summary for 1R37

• Entry DOI: 10.2210/pdb1r37/pdb
• Related: 1JVB 1NTO 1NVG
• Descriptor: NAD-dependent alcohol dehydrogenase, ZINC ION, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (5 entities in total)
• Functional Keywords: archaeon, zinc, nad(h) dependent, holoform, oxidoreductase
• Biological source: Sulfolobus solfataricus
• Total number of polymer chains: 2
• Total formula weight: 76999.77

Authors

Esposito, L.,Bruno, I.,Sica, F.,Raia, C.A.,Giordano, A.,Rossi, M.,Mazzarella, L.,Zagari, A. (deposition date: 2003-09-30, release date: 2004-02-10, Last modification date: 2023-10-25)

Primary citation

Esposito, L.,Bruno, I.,Sica, F.,Raia, C.A.,Giordano, A.,Rossi, M.,Mazzarella, L.,Zagari, A.
Crystal structure of a ternary complex of the alcohol dehydrogenase from Sulfolobus solfataricus
Biochemistry, 42:14397-14407, 2003

PubMed Abstract: 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.

PubMed: 14661950
DOI: 10.1021/bi035271b

Experimental method

X-RAY DIFFRACTION (2.3 Å)