X-ray crystal structure and small-angle X-ray scattering of sheep liver sorbitol dehydrogenase

Hemant P. Yennawar, Magda Mller, Richard Gillilan, Neela Yennawar

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

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 languageEnglish (US)
Pages (from-to)440-446
Number of pages7
JournalActa Crystallographica Section D: Biological Crystallography
Volume67
Issue number5
DOIs
StatePublished - May 1 2011

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L-Iditol 2-Dehydrogenase
Sheep
X-Rays
Liver
Catalytic Domain
Acetates
Molecular Models
Glycerol
Zinc
Water
Enzymes

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Medicine(all)

Cite this

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abstract = "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.",
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X-ray crystal structure and small-angle X-ray scattering of sheep liver sorbitol dehydrogenase. / Yennawar, Hemant P.; Mller, Magda; Gillilan, Richard; Yennawar, Neela.

In: Acta Crystallographica Section D: Biological Crystallography, Vol. 67, No. 5, 01.05.2011, p. 440-446.

Research output: Contribution to journalArticle

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