Structural basis for hijacking siderophore receptors by antimicrobial lasso peptides
Author(s)
Type
Journal Article
Abstract
The lasso peptide microcin J25 is known to hijack the siderophore receptor FhuA for initiating internalization. Here, we provide what is to our knowledge the first structural evidence on the recognition mechanism, and our biochemical data show that another closely related lasso peptide cannot interact with FhuA. Our work provides an explanation on the narrow activity spectrum of lasso peptides and opens the path to the development of new antibacterials.
Date Issued
2014-05-01
Date Acceptance
2014-03-13
Citation
Nature Chemical Biology, 2014, 10 (5), pp.340-342
ISSN
1552-4450
Publisher
Nature Research
Start Page
340
End Page
342
Journal / Book Title
Nature Chemical Biology
Volume
10
Issue
5
Copyright Statement
© 2014 Nature America, Inc. All rights reserved.
Sponsor
Biotechnology and Biological Sciences Research Council (BBSRC)
Identifier
http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000334672700006&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=1ba7043ffcc86c417c072aa74d649202
Grant Number
BB/H01778X/1
Subjects
Science & Technology
Life Sciences & Biomedicine
Biochemistry & Molecular Biology
OUTER-MEMBRANE PROTEIN
ESCHERICHIA-COLI K-12
MICROCIN J25
MASS-SPECTROMETER
CRYSTAL-STRUCTURE
TRANSPORTER FHUA
RNA-POLYMERASE
MODEL
TONB
PURIFICATION
Publication Status
Published
Date Publish Online
2014-04-06