2Q27
Crystal structure of oxalyl-coA decarboxylase from Escherichia coli
Summary for 2Q27
| Entry DOI | 10.2210/pdb2q27/pdb |
| Related | 2Q28 2Q29 |
| Descriptor | oxalyl-CoA decarboxylase, MAGNESIUM ION, SULFATE ION, ... (7 entities in total) |
| Functional Keywords | lyase; oxalyl-coa decarboxylase; oxalate degradation; thiamine diphosphate, lyase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 2 |
| Total formula weight | 123556.33 |
| Authors | Werther, T.,Zimmer, A.,Wille, G.,Hubner, G.,Weiss, M.S.,Konig, S. (deposition date: 2007-05-26, release date: 2008-06-03, Last modification date: 2024-02-21) |
| Primary citation | Werther, T.,Zimmer, A.,Wille, G.,Golbik, R.,Weiss, M.S.,Konig, S. New insights into structure-function relationships of oxalyl CoA decarboxylase from Escherichia coli. Febs J., 277:2628-2640, 2010 Cited by PubMed Abstract: The gene yfdU from Escherichia coli encodes a putative oxalyl coenzyme A decarboxylase, a thiamine diphosphate-dependent enzyme that is potentially involved in the degradation of oxalate. The enzyme has been purified to homogeneity. The kinetic constants for conversion of the substrate oxalyl coenzyme A by the enzyme in the absence and presence of the inhibitor coenzyme A, as well as in the absence and presence of the activator adenosine 5'-diphosphate, were determined using a novel continuous optical assay. The effects of these ligands on the solution and crystal structure of the enzyme were studied using small-angle X-ray scattering and X-ray crystal diffraction. Analyses of the obtained crystal structures of the enzyme in complex with the cofactor thiamine diphosphate, the activator adenosine 5'-diphosphate and the inhibitor acetyl coenzyme A, as well as the corresponding solution scattering patterns, allow comparison of the oligomer structures of the enzyme complexes under various experimental conditions, and provide insights into the architecture of substrate and effector binding sites. PubMed: 20553497DOI: 10.1111/j.1742-464X.2010.07673.x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.12 Å) |
Structure validation
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