Structure of theEscherichia coliArnAN-formyltransferase domain in complex withN5-formyltetrahydrofolate and UDP-Ara4N-Reference-Cited by-同舟云学术

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Structure of theEscherichia coliArnAN-formyltransferase domain in complex withN5-formyltetrahydrofolate and UDP-Ara4N

Published:2016-05-17 Issue:8 Volume:25 Page:1555-1562
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Genthe Nicholas A.¹,Thoden James B.¹,Holden Hazel M.¹

Affiliation:

1. Department of Biochemistry; University of Wisconsin; Madison Wisconsin 53706

Funder

The National Institutes of Health to H. M. H.

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Reference30 articles.

1. Molecular mechanisms of antibiotic resistance;Blair;Nat Rev Microbiol,2015

2. How do bacteria resist human antimicrobial peptides?;Peschel;Trends Microbiol,2002

3. Cationic antimicrobial peptides and their multifunctional role in the immune system;Scott;Crit Rev Immunol,2000

4. Lipopolysaccharide endotoxins;Raetz;Ann Rev Biochem,2002

5. Genetic and functional analysis of a PmrA-PmrB-regulated locus necessary for lipopolysaccharide modification, antimicrobial peptide resistance, and oral virulence of Salmonella enterica serovar typhimurium;Gunn;Infect Immun,2000

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2. Investigation of the enzymes required for the biosynthesis of an unusual formylated sugar in the emerging human pathogen Helicobacter canadensis;Protein Science;2021-08-31

3. Misannotations of the genes encoding sugar N ‐formyltransferases;Protein Science;2020-01-20

4. ArnD is a deformylase involved in polymyxin resistance;Chemical Communications;2020

5. Cryo-electron microscopy structures of ArnA, a key enzyme for polymyxin resistance, revealed unexpected oligomerizations and domain movements;Journal of Structural Biology;2019-10

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