2GCU
X-Ray Structure of Gene Product from Arabidopsis Thaliana At1g53580
Summary for 2GCU
| Entry DOI | 10.2210/pdb2gcu/pdb |
| Descriptor | Putative hydroxyacylglutathione hydrolase 3, FE (II) ION, SULFATE ION, ... (5 entities in total) |
| Functional Keywords | ethylmalonic encephalopathy, ethe1, structural genomics, protein structure initiative, psi, center for eukaryotic structural genomics, cesg, hydrolase |
| Biological source | Arabidopsis thaliana (thale cress) |
| Cellular location | Mitochondrion : Q9C8L4 |
| Total number of polymer chains | 4 |
| Total formula weight | 108986.98 |
| Authors | McCoy, J.G.,Wesenberg, G.E.,Phillips Jr., G.N.,Bitto, E.,Bingman, C.A.,Center for Eukaryotic Structural Genomics (CESG) (deposition date: 2006-03-14, release date: 2006-04-18, Last modification date: 2024-10-30) |
| Primary citation | McCoy, J.G.,Bingman, C.A.,Bitto, E.,Holdorf, M.M.,Makaroff, C.A.,Phillips, G.N. Structure of an ETHE1-like protein from Arabidopsis thaliana. ACTA CRYSTALLOGR.,SECT.D, 62:964-970, 2006 Cited by PubMed 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. PubMed: 16929096DOI: 10.1107/S0907444906020592 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.477 Å) |
Structure validation
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