type	Journal Article
authors	Noland, B.W., Newman, J.M.; Hendle, J.; Badger J.; Christopher, J.A.; Tresser, J.; Buchanan, M.D.; Wright, T.A.; Rutter, M.E.; Sanderson, W.E.; Muller-Dieckmann, H.J.; Gajiwala, K.S.; Buchanan, S.G.
title	Structural studies of Salmonella typhimurium ArnB (PmrH) aminotransferase: a 4-amino-4-deoxy-L-arabinose lipopolysaccharide-modifying enzyme
journal	Structure (Camb)
Activity	2.6.1.87
Family	2.6.1.87
sel	selected
ui	12429098
year	(2002)
volume	10
number	11
pages	1569-80
abstract	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 UDP-linked ketopyranose molecule to form UDP-4-amino-4-deoxy-L-arabinose represents a key step in the lipid A modification pathway. Structural and functional studies of the ArnB aminotransferase were undertaken by combining X-ray crystallography with biochemical analyses. High-resolution crystal structures were solved for two native forms and one covalently inhibited form of S. typhimurium ArnB. These structures permitted identification of key residues involved in substrate binding and catalysis, including a rarely observed nonprolyl cis peptide bond in the active site.
last changed	2014/02/20 11:36