Abstract
The structure and conformation of antibiotic chryscandin, a structural analog of the terminus 3′-aminoacyladenylate moiety of tRNA, has been determined. The crystals belong to orthorhombic space group P212121. The structure was refined to an R value of 0.065 for 1872 reflections. The structure and conformation has been compared with that of puromycin. The sugar pucker is different from that of puromycin, thus creating different orientation of peptide group with respect to nucleoside. All the water molecules are involved in hydrogen bonding. The crystal is also stabilized by stacking of adenine bases and p-methoxyphenyl rings. The results will be helpful in understanding structure-biological activity relationships, identification of inhibitors of metallopeptidases, and how chryscandin interacts with ribosomal units.
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This paper is dedicated to the memory of Prof. M. Sundaralingam, who died in the tsunami earthquake in 2004 on a visit to his native Sri Lanka. He was deeply involved in the study of nucleoside antibiotics.
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Liu, M., Arora, S. Structural Investigations of Mode of Action of Drugs: Structure and Conformation of a Novel Peptidyl Nucleoside Antibiotic Chryscandin Hydrochloride Pentahydrate. J Antibiot 61, 322–325 (2008). https://doi.org/10.1038/ja.2008.46
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DOI: https://doi.org/10.1038/ja.2008.46