Structural highlights
Function
[DHSO_RHOSH] Catalyzes the oxidation of D-glucitol (sorbitol) to D-fructose, galactitol to D-tagatose and of L-iditol.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Recombinant sorbitol dehydrogenase (SDH) from Rhodobacter sphaeroides has been crystallized in the absence of the cofactor NAD(H) and its structure determined to 2.4 A resolution using molecular replacement (refined R and R free factors of 18.8 and 23.8%, respectively). As expected from the sequence and shown by the conserved fold, SDH can be assigned to the short-chain dehydrogenase/reductase protein family. The cofactor NAD and the substrate sorbitol have been modelled into the structure and the active-site architecture, which displays the highly conserved catalytic tetrad of Asn-Ser-Tyr-Lys residues, is discussed in relation to the enzyme mechanism. This is the first structure of a bacterial SDH belonging to the SDR family.
Structure of zinc-independent sorbitol dehydrogenase from Rhodobacter sphaeroides at 2.4 A resolution.,Philippsen A, Schirmer T, Stein MA, Giffhorn F, Stetefeld J Acta Crystallogr D Biol Crystallogr. 2005 Apr;61(Pt 4):374-9. Epub 2005, Mar 24. PMID:15805591[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Philippsen A, Schirmer T, Stein MA, Giffhorn F, Stetefeld J. Structure of zinc-independent sorbitol dehydrogenase from Rhodobacter sphaeroides at 2.4 A resolution. Acta Crystallogr D Biol Crystallogr. 2005 Apr;61(Pt 4):374-9. Epub 2005, Mar 24. PMID:15805591 doi:10.1107/S0907444904034390
