title: Structure of aldose reductase from Giardia lamblia.
abstract: Giardia lamblia is an anaerobic aerotolerant eukaryotic parasite of the intestines. It is believed to have diverged early from eukarya during evolution and is thus lacking in many of the typical eukaryotic organelles and biochemical pathways. Most conspicuously, mitochondria and the associated machinery of oxidative phosphorylation are absent; instead, energy is derived from substrate-level phosphorylation. Here, the 1.75 Å resolution crystal structure of G. lamblia aldose reductase heterologously expressed in Escherichia coli is reported. As in other oxidoreductases, G. lamblia aldose reductase adopts a TIM-barrel conformation with the NADP(+)-binding site located within the eight β-strands of the interior.
authors: Seattle Structural Genomics Center for Infectious Disease, USA. micah.ferrell@seattlebiomed.org
authors: M
authors: M
authors: Ferrell
authors: J
authors: J
authors: Abendroth
authors: Y
authors: Y
authors: Zhang
authors: B
authors: B
authors: Sankaran
authors: T E
authors: TE
authors: Edwards
authors: B L
authors: BL
authors: Staker
authors: W C
authors: WC
authors: Van Voorhis
authors: L J
authors: LJ
authors: Stewart
authors: P J
authors: PJ
authors: Myler
mesh_terms: D000449:Aldehyde Reductase / Q000737:chemistry*; D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D016829:Giardia lamblia / Q000201:enzymology*; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity
chemical_list: D000449:Aldehyde Reductase