1jvb
From Proteopedia
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ALCOHOL DEHYDROGENASE FROM THE ARCHAEON SULFOLOBUS SOLFATARICUS
Overview
The crystal structure of a medium-chain NAD(H)-dependent alcohol, dehydrogenase (ADH) from an archaeon has been solved by multiwavelength, anomalous diffraction, using a selenomethionine-substituted enzyme. The, protein (SsADH), extracted from the hyperthermophilic organism Sulfolobus, solfataricus, is a homo-tetramer with a crystallographic 222 symmetry., Despite the low level of sequence identity, the overall fold of the, monomer is similar to that of the other homologous ADHs of known, structure. However, a significant difference is the orientation of the, catalytic domain relative to the coenzyme-binding domain that results in a, larger interdomain cleft. At the bottom of this cleft, the catalytic zinc, ion is coordinated tetrahedrally and lacks the zinc-bound water molecule, that is usually found in ADH apoform structures. The fourth coordination, position is indeed occupied by a Glu residue, as found in bacterial, tetrameric ADHs. Other differences are found in the architecture of the, substrate pocket whose entrance is more restricted than in other ADHs., SsADH is the first tetrameric ADH X-ray structure containing a second zinc, ion playing a structural role. This latter metal ion shows a peculiar, coordination, with a glutamic acid residue replacing one of the four, cysteine ligands that are highly conserved throughout the structural, zinc-containing dimeric ADHs.
About this Structure
1JVB is a Single protein structure of sequence from Sulfolobus solfataricus with as ligand. Active as Alcohol dehydrogenase, with EC number 1.1.1.1 Known structural/functional Sites: and . Full crystallographic information is available from OCA.
Reference
Crystal structure of the alcohol dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus at 1.85 A resolution., Esposito L, Sica F, Raia CA, Giordano A, Rossi M, Mazzarella L, Zagari A, J Mol Biol. 2002 Apr 26;318(2):463-77. PMID:12051852
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