X-ray crystal structure and small-angle X-ray scattering of sheep liver sorbitol dehydrogenase
Research output: Contribution to journal › Journal article › Research › peer-review
The X-ray crystal structure of sheep liver sorbitol dehydrogenase (slSDH) has been determined using the crystal structure of human sorbitol dehydrogenase (hSDH) as a molecular-replacement model. slSDH crystallized in space group I222 with one monomer in the asymmetric unit. A conserved tetramer that superposes well with that seen in hSDH (despite belonging to a different space group) and obeying the 222 crystal symmetry is seen in slSDH. An acetate molecule is bound in the active site, coordinating to the active-site zinc through a water molecule. Glycerol, a substrate of slSDH, also occupies the substrate-binding pocket together with the acetate designed by nature to fit large polyol substrates. The substrate-binding pocket is seen to be in close proximity to the tetramer interface, which explains the need for the structural integrity of the tetramer for enzyme activity. Small-angle X-ray scattering was also used to identify the quaternary structure of the tetramer of slSDH in solution.
Original language | English |
---|---|
Journal | Acta Crystallographica. Section D: Biological Crystallography |
Volume | 67 |
Issue number | Pt 5 |
Pages (from-to) | 440-446 |
ISSN | 0907-4449 |
DOIs | |
Publication status | Published - May 2011 |
Bibliographical note
Keywords: sheep liver sorbitol dehydrogenase; 3qe3
- Former Faculty of Pharmaceutical Sciences
Research areas
ID: 38145892