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. 2005 Apr;61(Pt 4):374-9.
doi: 10.1107/S0907444904034390. Epub 2005 Mar 24.

Structure of zinc-independent sorbitol dehydrogenase from Rhodobacter sphaeroides at 2.4 A resolution

Ansgar Philippsen  1 , Tilman Schirmer, Martin A Stein, Friedrich Giffhorn, Jörg Stetefeld
Affiliations

Structure of zinc-independent sorbitol dehydrogenase from Rhodobacter sphaeroides at 2.4 A resolution

Ansgar Philippsen et al. Acta Crystallogr D Biol Crystallogr. 2005 Apr.

Abstract

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.

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