3TM7
Processed Aspartate Decarboxylase Mutant with Asn72 mutated to Ala
Summary for 3TM7
| Entry DOI | 10.2210/pdb3tm7/pdb |
| Related | 1AW8 1PPY 1PQE 1PQF 1PQH 1PYQ |
| Descriptor | Aspartate 1-decarboxylase beta chain, Aspartate 1-decarboxylase alpha chain, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | auto-processing, lyase, pyruvoyl |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 4 |
| Total formula weight | 28131.79 |
| Authors | Webb, M.E.,Lobley, C.M.C.,Soliman, F.,Kilkenny, M.L.,Smith, A.G.,Abell, C.,Blundell, T.L. (deposition date: 2011-08-31, release date: 2012-04-11, Last modification date: 2024-02-28) |
| Primary citation | Webb, M.E.,Lobley, C.M.,Soliman, F.,Kilkenny, M.L.,Smith, A.G.,Blundell, T.L.,Abell, C. Structure of Escherichia coli aspartate alpha-decarboxylase Asn72Ala: probing the role of Asn72 in pyruvoyl cofactor formation Acta Crystallogr.,Sect.F, 68:414-417, 2012 Cited by PubMed Abstract: The crystal structure of the Asn72Ala site-directed mutant of Escherichia coli aspartate α-decarboxylase (ADC) has been determined at 1.7 Å resolution. The refined structure is consistent with the presence of a hydrolysis product serine in the active site in place of the pyruvoyl group required for catalysis, which suggests that the role of Asn72 is to protect the ester formed during ADC activation from hydrolysis. In previously determined structures of activated ADC, including the wild type and other site-directed mutants, the C-terminal region of the protein is disordered, but in the Asn72Ala mutant these residues are ordered owing to an interaction with the active site of the neighbouring symmetry-related multimer. PubMed: 22505409DOI: 10.1107/S1744309112009487 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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