Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Escherichia coli |
Crystallization (Comment) | Organism |
---|---|
to 1.4 A resolution. The overall structure of SSADH shares the general fold of ALDH classes 1 and 2. The SSADH monomer is composed of three domains; an N-terminal NAD(P)-binding domain of residues 1Β125, 148Β256, and 457Β472, a catalytic domain of residues 257Β456, and an oligomerization domain of residues 126Β147 and 473Β482. The catalytic loop of Escherichia coli SSADH, unlike that of human SSADH, does not undergo disulfide bond-mediated structural changes upon changes of environmental redox status. The protein is not regulated via redox-switch modulation. A difference in the conformation of the connecting loop beta15Βbeta16 causes the formation of a water molecule-mediated hydrogen bond network between the connecting loop and the catalytic loop in Escherichia coli SSADH | Escherichia coli |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytosol | - |
Escherichia coli | 5829 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |