X-ray crystal structure and small-angle X-ray scattering of sheep liver sorbitol dehydrogenase
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X-ray crystal structure and small-angle X-ray scattering of sheep liver sorbitol dehydrogenase. / Yennawar, Hemant; Møller, Magda; Gillilan, Richard; Yennawar, Neela.
In: Acta Crystallographica. Section D: Biological Crystallography, Vol. 67, No. Pt 5, 05.2011, p. 440-446.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - X-ray crystal structure and small-angle X-ray scattering of sheep liver sorbitol dehydrogenase
AU - Yennawar, Hemant
AU - Møller, Magda
AU - Gillilan, Richard
AU - Yennawar, Neela
N1 - Keywords: sheep liver sorbitol dehydrogenase; 3qe3
PY - 2011/5
Y1 - 2011/5
N2 - 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.
AB - 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.
KW - Former Faculty of Pharmaceutical Sciences
U2 - 10.1107/S0907444911007815
DO - 10.1107/S0907444911007815
M3 - Journal article
C2 - 21543846
VL - 67
SP - 440
EP - 446
JO - Acta Crystallographica Section D: Structural Biology
JF - Acta Crystallographica Section D: Structural Biology
SN - 2059-7983
IS - Pt 5
ER -
ID: 38145892