The structural basis for substrate versatility of chloramphenicol acetyltransferase CATI
نویسندگان
چکیده
منابع مشابه
The structural basis for substrate versatility of chloramphenicol acetyltransferase CATI.
Novel antibiotics are needed to overcome the challenge of continually evolving bacterial resistance. This has led to a renewed interest in mechanistic studies of once popular antibiotics like chloramphenicol (CAM). Chloramphenicol acetyltransferases (CATs) are enzymes that covalently modify CAM, rendering it inactive against its target, the ribosome, and thereby causing resistance to CAM. Of th...
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Nα-acetyltransferases (Nats) possess a wide range of important biological functions. Their structures can vary according to the first two residues of their substrate. However, the mechanisms of substrate recognition and catalysis of Nats are elusive. Here, we present two structure of Sulfolobus solfataricus Ard1 (SsArd1), a member of the NatA family, at 2.13 and 1.84 Å. Both structures contain ...
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ژورنال
عنوان ژورنال: Protein Science
سال: 2012
ISSN: 0961-8368
DOI: 10.1002/pro.2036