PMID:9782055
| Citation |
Colovos, C, Cascio, D and Yeates, TO (1998) The 1.8 A crystal structure of the ycaC gene product from Escherichia coli reveals an octameric hydrolase of unknown specificity. Structure 6:1329-37 |
|---|---|
| Abstract |
The ycaC gene comprises a 621 base pair open reading frame in Escherichia coli. The ycaC gene product (ycaCgp) is uncharacterized and has no assigned function. The closest sequence homologs with an assigned function belong to a family of bacterial hydrolases that catalyze isochorismatase-like reactions, but these have only low sequence similarity to ycaCgp (approximately 20% amino acid identity). The ycaCgp was obtained and identified during crystallization trials of an unrelated E. coli protein with which it co-purified. |
| Links | |
| Keywords |
Amidohydrolases/chemistry; Amino Acid Sequence; Arthrobacter/enzymology; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Crystallography, X-Ray; Escherichia coli/enzymology; Escherichia coli Proteins; Hydrolases/chemistry; Hydrolases/metabolism; Macromolecular Substances; Molecular Sequence Data; Protein Conformation; Protein Structure, Secondary; Sequence Alignment; Sequence Homology, Amino Acid; Substrate Specificity |
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