Structural studies of Salmonella typhimurium ArnB (PmrH) aminotransferase:: A 4-amino-4-deoxy-L-arabinose lipopolysaccharide-modifying enzyme

被引：67

作者：

Noland, BW ^{[1
]}

Newman, JM ^{[1
]}

Hendle, J ^{[1
]}

Badger, J ^{[1
]}

Christopher, JA ^{[1
]}

Tresser, J ^{[1
]}

Buchanan, MD ^{[1
]}

Wright, TA ^{[1
]}

Rutter, ME ^{[1
]}

Sanderson, WE ^{[1
]}

Müller-Dieckmann, HJ ^{[1
]}

Gajiwala, KS ^{[1
]}

Buchanan, SG ^{[1
]}

机构：

[1] Struct Genomix, San Diego, CA 92121 USA

来源：

STRUCTURE | 2002年 / 10卷 / 11期

关键词：

D O I：

10.1016/S0969-2126(02)00879-1

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：1569 / 1580

页数：12

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