PMID:11856852
| Citation |
Momany, C, Levdikov, V, Blagova, L and Crews, K (2002) Crystallization of diaminopimelate decarboxylase from Escherichia coli, a stereospecific D-amino-acid decarboxylase. Acta Crystallogr. D Biol. Crystallogr. 58:549-52 |
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| Abstract |
The final step in lysine biosynthesis in bacteria, the conversion of meso-diaminopimelate to L-lysine, is catalyzed by the only known D-amino-acid decarboxylase, diaminopimelate decarboxylase (DDC). The Escherichia coli DDC has been cloned, overexpressed in E. coli with a carboxy-terminal polyhistidine purification tag and crystallized from lithium sulfate. The protein is intensely yellow, owing to the pyridoxal-5'-phosphate cofactor, and is enzymatically active. Large well ordered crystals, belonging to space group P6(1)22 with unit-cell parameters a = b = 98.6, c = 177 A, make high-resolution X-ray diffraction studies possible to characterize the residues important in stereospecific decarboxylation and reprotonation during catalytic turnover. |
| Links | |
| Keywords |
Bacterial Proteins; Carboxy-Lyases/chemistry; Carboxy-Lyases/genetics; Cloning, Molecular; Crystallization; Crystallography, X-Ray; Decarboxylation; Escherichia coli/chemistry; Escherichia coli/enzymology; Escherichia coli/genetics; Protein Conformation |
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