Structures of aminoarabinose transferase ArnT suggest a molecular basis for lipid A glycosylation

Autor:	Meagan Belcher Dufrisne, Jeremie Vendome, Carmen M. Herrera, Surajit Banerjee, Lawrence Shapiro, David Tomasek, Vasileios I. Petrou, M. Stephen Trent, Kanagalaghatta R. Rajashankar, Burkhard Rost, Kathryn M. Schultz, Brian Kloss, Oliver B. Clarke, Edda Kloppmann, Filippo Mancia, Candice S. Klug
Rok vydání:	2016
Předmět:	0301 basic medicine Glycosylation 030106 microbiology Plasma protein binding Crystallography X-Ray Article Catalysis Protein Structure Secondary Substrate Specificity Lipid A 03 medical and health sciences chemistry.chemical_compound Protein structure Bacterial Proteins Polyisoprenyl Phosphates Catalytic Domain Transferase Pentosyltransferases Polymyxins Multidisciplinary biology Cupriavidus metallidurans Cupriavidus Active site Amino Sugars biology.organism_classification Arabinose Protein Structure Tertiary 030104 developmental biology Biochemistry chemistry Mutagenesis Mutation biology.protein lipids (amino acids peptides and proteins) Bacterial outer membrane Protein Binding
Zdroj:	Science. 351:608-612
ISSN:	1095-9203 0036-8075
Popis:	A bacterial defense mechanism Polymyxins are antibiotics that disrupt the bacterial cell membrane and are used to treat multidrug-resistant infections. A bacterial enzyme called ArnT can mediate resistance to polymyxins by transferring a sugar group from a lipid carrier to lipid A, a component of the bacterial outer membrane. Petrou et al. described structures of ArnT alone and in complex with a lipid carrier and identified a cavity where lipid A probably binds. Insights into the enzyme mechanism could be exploited to design drugs that combat polymyxin resistance. Science , this issue p. 608
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::317d8bbffc9a98043fb8d6065178c70d https://doi.org/10.1126/science.aad1172 Zobrazit plný text záznamu Plný text ve formátu PDF