Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1NTO

N249Y MUTANT OF ALCOHOL DEHYDROGENASE FROM THE ARCHAEON SULFOLOBUS SOLFATARICUS-MONOCLINIC CRYSTAL FORM

Summary for 1NTO
Entry DOI10.2210/pdb1nto/pdb
Related1JVB 1nvg
DescriptorNAD-dependent alcohol dehydrogenase, ZINC ION (3 entities in total)
Functional Keywordsarchaeon, nad(h)-dependent, mutant, oxidoreductase
Biological sourceSulfolobus solfataricus
Total number of polymer chains6
Total formula weight226772.47
Authors
Esposito, L.,Bruno, I.,Sica, F.,Raia, C.A.,Giordano, A.,Rossi, M.,Mazzarella, L.,Zagari, A. (deposition date: 2003-01-30, release date: 2003-08-26, Last modification date: 2023-08-16)
Primary citationEsposito, L.,Bruno, I.,Sica, F.,Raia, C.A.,Giordano, A.,Rossi, M.,Mazzarella, L.,Zagari, A.
Structural study of a single-point mutant of Sulfolobus solfataricus alcohol dehydrogenase with enhanced activity.
Febs Lett., 539:14-18, 2003
Cited by
PubMed Abstract: 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.
PubMed: 12650918
DOI: 10.1016/S0014-5793(03)00173-X
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.94 Å)
Structure validation

238582

数据于2025-07-09公开中

PDB statisticsPDBj update infoContact PDBjnumon