Structures of aminoarabinose transferase ArnT suggest a molecular basis for lipid A glycosylation
Structures of aminoarabinose transferase ArnT suggest a molecular basis for lipid A glycosylation
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Author / Creator
Petrou, Vasileios I. , Herrera, Carmen M. , Schultz, Kathryn M. , Clarke, Oliver B. , Vendome, Jérémie , Tomasek, David , Banerjee, Surajit , Rajashankar, Kanagalaghatta R. , Dufrisne, Meagan Belcher , Kloss, Brian , Kloppmann, Edda , Rost, Burkhard , Klug, Candice S. , Trent, M. Stephen , Shapiro, Lawrence , Mancia, Filippo and Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Publisher
United States: American Association for the Advancement of Science
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Language
English
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Publisher
United States: American Association for the Advancement of Science
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Contents
Polymyxins are antibiotics used in the last line of defense to combat multidrug-resistant infections by Gram-negative bacteria. Polymyxin resistance arises through charge modification of the bacterial outer membrane with the attachment of the cationic sugar 4-amino-4-deoxy-L-arabinose to lipid A, a reaction catalyzed by the integral membrane lipid-...
Alternative Titles
Full title
Structures of aminoarabinose transferase ArnT suggest a molecular basis for lipid A glycosylation
Authors, Artists and Contributors
Author / Creator
Herrera, Carmen M.
Schultz, Kathryn M.
Clarke, Oliver B.
Vendome, Jérémie
Tomasek, David
Banerjee, Surajit
Rajashankar, Kanagalaghatta R.
Dufrisne, Meagan Belcher
Kloss, Brian
Kloppmann, Edda
Rost, Burkhard
Klug, Candice S.
Trent, M. Stephen
Shapiro, Lawrence
Mancia, Filippo
Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
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Record Identifier
TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4963604
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4963604
Other Identifiers
ISSN
0036-8075,1095-9203
E-ISSN
1095-9203
DOI
10.1126/science.aad1172