Dimerization of TonB Is Not Essential for Its Binding to the Outer Membrane Siderophore Receptor FhuA of Escherichia coli
Open Access
- 1 March 2004
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 279 (11) , 9978-9986
- https://doi.org/10.1074/jbc.m311720200
Abstract
No abstract availableKeywords
This publication has 53 references indexed in Scilit:
- Studies on transformation of Escherichia coli with plasmidsPublished by Elsevier ,2006
- FepA with Globular Domain Deletions Lacks ActivityJournal of Bacteriology, 2002
- FhuA Barrel-Cork Hybrids Are Active Transporters and ReceptorsJournal of Bacteriology, 2001
- Conserved Residues Ser16 and His20 and Their Relative Positioning Are Essential for TonB Activity, Cross-linking of TonB with ExbB, and the Ability of TonB to Respond to Proton Motive ForceJournal of Biological Chemistry, 2001
- Transmembrane Signaling across the Ligand-Gated FhuA ReceptorCell, 1998
- Refinement of Macromolecular Structures by the Maximum-Likelihood MethodActa Crystallographica Section D-Biological Crystallography, 1997
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994
- ErratumMolecular Microbiology, 1994
- In vivo evidence for FhuA outer membrane receptor interaction with the TonB inner membrane protein of Escherichia coliFEBS Letters, 1990
- Sequence‐imposed structural constraints in the TonB protein of E. coliFEBS Letters, 1986