1nvg
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N249Y MUTANT OF THE ALCOHOL DEHYDROGENASE FROM THE ARCHAEON SULFOLOBUS SOLFATARICUS-TETRAGONAL CRYSTAL FORM
OverviewOverview
Alcohol dehydrogenase from Sulfolobus solfataricus (SsADH) is the only, enzyme from Archaea among the structurally studied members of the, medium-chain ADH family described so far. Here, we present the, three-dimensional structure of the apo form of the mutant N249Y which, exhibits increased catalytic activity when compared to the wild-type, enzyme. The substitution, located in the coenzyme binding domain, decreases the affinity for NAD(H) cofactor. The rearrangement of segments, 248-250 and 270-275, induced by the mutation, suggests an explanation for, the lower coenzyme affinity. This study also highlights the role in SsADH, catalysis of the flexible loops located at the interface between the, catalytic and the coenzyme domains.
About this StructureAbout this Structure
1NVG is a Single protein structure of sequence from Sulfolobus solfataricus with ZN as ligand. Active as Alcohol dehydrogenase, with EC number 1.1.1.1 Structure known Active Site: ZNS. Full crystallographic information is available from OCA.
ReferenceReference
Structural study of a single-point mutant of Sulfolobus solfataricus alcohol dehydrogenase with enhanced activity., Esposito L, Bruno I, Sica F, Raia CA, Giordano A, Rossi M, Mazzarella L, Zagari A, FEBS Lett. 2003 Mar 27;539(1-3):14-8. PMID:12650918
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