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Structure of aldose reductase from Giardia lamblia.

TitleStructure of aldose reductase from Giardia lamblia.
Publication TypeJournal Article
Year of Publication2011
AuthorsFerrell, M, Abendroth, J, Zhang, Y, Sankaran, B, Edwards, TE, Staker, BL, Van Voorhis, WC, Stewart, LJ, Myler, PJ
JournalActa Crystallogr Sect F Struct Biol Cryst Commun
Volume67
IssuePt 9
Pagination1113-7
Date Published2011 Sep 1
ISSN1744-3091
KeywordsAldehyde Reductase, Amino Acid Sequence, Crystallography, X-Ray, Giardia lamblia, Humans, Models, Molecular, Molecular Sequence Data, Protein Structure, Quaternary, Protein Structure, Tertiary, Sequence Alignment, Sequence Homology, Amino Acid, Substrate Specificity
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.

DOI10.1107/S1744309111030879
Alternate JournalActa Crystallogr. Sect. F Struct. Biol. Cryst. Commun.
PubMed ID21904059