期刊
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY
卷 62, 期 -, 页码 964-970出版社
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S0907444906020592
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资金
- NCI NIH HHS [Y1-CO-1020] Funding Source: Medline
- NIGMS NIH HHS [Y1-GM-1104, P50 GM 64598, U54 GM 074901] Funding Source: Medline
- NLM NIH HHS [T15 LM007359] Funding Source: Medline
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.
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