Skip to content Skip to navigation
University of Warwick
  • Study
  • |
  • Research
  • |
  • Business
  • |
  • Alumni
  • |
  • News
  • |
  • About

University of Warwick
Publications service & WRAP

Highlight your research

  • WRAP
    • Home
    • Search WRAP
    • Browse by Warwick Author
    • Browse WRAP by Year
    • Browse WRAP by Subject
    • Browse WRAP by Department
    • Browse WRAP by Funder
    • Browse Theses by Department
  • Publications Service
    • Home
    • Search Publications Service
    • Browse by Warwick Author
    • Browse Publications service by Year
    • Browse Publications service by Subject
    • Browse Publications service by Department
    • Browse Publications service by Funder
  • Help & Advice
University of Warwick

The Library

  • Login
  • Admin

Functional and structural analysis of the siderophore synthetase AsbB through reconstitution of the petrobactin biosynthetic pathway from bacillus anthracis

Tools
- Tools
+ Tools

Nusca, T. D., Kim, Y., Maltseva, N., Lee, J. Y., Eschenfeldt, W., Stols, L., Schofield, M. M., Scaglione, J. B., Dixon, S. D., Oves-Costales, Daniel, Challis, G. L., Hanna, P. C., Pfleger, B. F., Joachimiak, A. and Sherman, D. H. (2012) Functional and structural analysis of the siderophore synthetase AsbB through reconstitution of the petrobactin biosynthetic pathway from bacillus anthracis. Journal of Biological Chemistry, Volume 287 (Number 19). pp. 16058-16072. doi:10.1074/jbc.M112.359349 ISSN 0021-9258.

Research output not available from this repository.

Request-a-Copy directly from author or use local Library Get it For Me service.

Official URL: http://dx.doi.org/10.1074/jbc.M112.359349

Request Changes to record.

Abstract

Background: asbABCDEF mediates petrobactin production and facilitates anthrax virulence.

Results: Purified AsbA-E proteins reconstituted petrobactin assembly in vitro. The crystal structure and enzymatic studies of AsbB highlight its function and role in the siderophore pathway.

Conclusion: AsbB characterization demonstrated reaction flexibility and substrate positions in the binding pocket.

Significance: Siderophore synthetases represent promising antimicrobial targets, and characterization of these versatile enzymes enables creation of novel compounds.

Item Type: Journal Article
Divisions: Faculty of Science, Engineering and Medicine > Science > Chemistry
Journal or Publication Title: Journal of Biological Chemistry
Publisher: American Society for Biochemistry and Molecular Biology
ISSN: 0021-9258
Official Date: 4 May 2012
Dates:
DateEvent
4 May 2012Published
Volume: Volume 287
Number: Number 19
Page Range: pp. 16058-16072
DOI: 10.1074/jbc.M112.359349
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Restricted or Subscription Access

Request changes or add full text files to a record

Repository staff actions (login required)

View Item View Item
twitter

Email us: wrap@warwick.ac.uk
Contact Details
About Us