Title | Structure of an ETHE1-like protein from Arabidopsis thaliana. |
Publication Type | Journal Article |
Year of Publication | 2006 |
Authors | McCoy JG, Bingman CA, Bitto E, Holdorf MM, Makaroff CA, Phillips GN |
Journal | Acta Crystallogr D Biol Crystallogr |
Volume | 62 |
Issue | Pt 9 |
Pagination | 964-70 |
Date Published | 2006 Sep |
ISSN | 0907-4449 |
Keywords | Amino 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. |
DOI | 10.1107/S0907444906020592 |
Alternate Journal | Acta Crystallogr. D Biol. Crystallogr. |
PubMed ID | 16929096 |
Grant List | P50 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 |