Department of Anesthesiology

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Structure of an ETHE1-like protein from Arabidopsis thaliana.

TitleStructure of an ETHE1-like protein from Arabidopsis thaliana.
Publication TypeJournal Article
Year of Publication2006
AuthorsMcCoy JG, Bingman CA, Bitto E, Holdorf MM, Makaroff CA, Phillips GN
JournalActa Crystallogr D Biol Crystallogr
Volume62
IssuePt 9
Pagination964-70
Date Published2006 Sep
ISSN0907-4449
KeywordsAmino Acid Sequence, Arabidopsis, Binding Sites, Brain Diseases, Cloning, Molecular, Crystallography, X-Ray, Humans, Mitochondrial Proteins, Models, Molecular, Molecular Sequence Data, Nucleocytoplasmic Transport Proteins, Plant Proteins, Protein Conformation, Protein Structure, Secondary, Protein Structure, Tertiary, Sequence Homology, Amino Acid, X-Ray Diffraction
Abstract

The protein product of gene At1g53580 from Arabidopsis thaliana possesses 54% sequence identity to a human enzyme that has been implicated in the rare disorder ethylmalonic encephalopathy. The structure of the At1g53580 protein has been solved to a nominal resolution of 1.48 Angstrom. This structure reveals tertiary structure differences between the ETHE1-like enzyme and glyoxalase II enzymes that are likely to account for differences in reaction chemistry and multimeric state between the two types of enzymes. In addition, the Arabidopsis ETHE1 protein is used as a model to explain the significance of several mutations in the human enzyme that have been observed in patients with ethylmalonic encephalopathy.

DOI10.1107/S0907444906020592
Alternate JournalActa Crystallogr. D Biol. Crystallogr.
PubMed ID16929096
Grant ListP50 GM 64598 / GM / NIGMS NIH HHS / United States
T15 LM007359 / LM / NLM NIH HHS / United States
U54 GM 074901 / GM / NIGMS NIH HHS / United States
Y1-CO-1020 / CO / NCI NIH HHS / United States
Y1-GM-1104 / GM / NIGMS NIH HHS / United States