Structural Studies of Salmonella typhimurium ArnB (PmrH) Aminotransferase : A 4-Amino-4-Deoxy-L-Arabinose Lipopolysaccharide-Modifying Enzyme

• Published in: Structure (London) Vol. 10; no. 11; pp. 1569 - 1580
• Main Authors: Noland, Brian W., Newman, Janet M., Hendle, Jörg, Badger, John, Christopher, Jon A., Tresser, Jason, Buchanan, Michelle D., Wright, Tobi A., Rutter, Marc E., Sanderson, Wendy E., Müller-Dieckmann, Hans-Joachim, Gajiwala, Ketan S., Buchanan, Sean G.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.11.2002
• Subjects: Amino Acid Sequence; aminoarabinose; aminotransferase; Binding Sites; Catalysis; cis peptide; Crystallography, X-Ray; Cycloserine - chemistry; Escherichia coli - metabolism; lipid A; lipopolysaccharide; Lipopolysaccharides - metabolism; Mass Spectrometry; Models, Chemical; Models, Molecular; Molecular Sequence Data; PLP; Protein Folding; Protein Structure, Secondary; Pyridoxamine - analogs & derivatives; Pyridoxamine - chemistry; Salmonella typhimurium - enzymology; Sequence Homology, Amino Acid; Structure-Activity Relationship; Transaminases - chemistry; cis peptide; aminotransferase; lipopolysaccharide; PLP; lipid A; aminoarabinose

Lipid A modification with 4-amino-4-deoxy-L-arabinose confers on certain pathogenic bacteria, such as Salmonella, resistance to cationic antimicrobial peptides, including those derived from the innate immune system. ArnB catalysis of amino group transfer from glutamic acid to the 4″-position of a UD...