Structural basis for iron binding and release by a novel class of periplasmic iron-binding proteins found in gram-negative pathogens

Shouldice, Stephen R., Skene, Robert J., Dougan, Douglas R., Snell, Gyorgy, McRee, Duncan E., Schryvers, Anthony B. and Tari, Leslie W. (2004) Structural basis for iron binding and release by a novel class of periplasmic iron-binding proteins found in gram-negative pathogens. Journal of Bacteriology, 186 12: 3903-3910. doi:10.1128/JB.186.12.3903-3910.2004

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Author Shouldice, Stephen R.
Skene, Robert J.
Dougan, Douglas R.
Snell, Gyorgy
McRee, Duncan E.
Schryvers, Anthony B.
Tari, Leslie W.
Title Structural basis for iron binding and release by a novel class of periplasmic iron-binding proteins found in gram-negative pathogens
Journal name Journal of Bacteriology   Check publisher's open access policy
ISSN 0021-9193
1098-5530
Publication date 2004-06
Sub-type Article (original research)
DOI 10.1128/JB.186.12.3903-3910.2004
Open Access Status File (Publisher version)
Volume 186
Issue 12
Start page 3903
End page 3910
Total pages 8
Place of publication Washington, DC, United States
Publisher American Society for Microbiology
Language eng
Abstract We have determined the 1.35- and 1.45-Angstrom structures, respectively, of closed and open iron-loaded forms of Mannheimia haemolytica ferric ion-binding protein A. M. haemolytica is the causative agent in the economically important and fatal disease of cattle termed shipping fever. The periplasmic iron-binding protein of this gram-negative bacterium, which has homologous counterparts in many other pathogenic species, performs a key role in iron acquisition from mammalian host serum iron transport proteins and is essential for the survival of the pathogen within the host. The ferric (Fe3+) ion in the closed structure is bound by a novel asymmetric constellation of four ligands, including a synergistic carbonate anion. The open structure is ligated by three tyrosyl residues and a dynamically disordered solvent-exposed anion. Our results clearly implicate the synergistic anion as the primary mediator of global protein conformation and provide detailed insights into the molecular mechanisms of iron binding and release in the periplasm.
Keyword Microbiology
Pasteurella-haemolytica
Haemophilus-influenzae
Bacterial Transferrin
Human Lactoferrin
Identification
Acquisition
Neisseria
Refinement
Infection
Receptors
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collections: Excellence in Research Australia (ERA) - Collection
Institute for Molecular Bioscience - Publications
 
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Created: Fri, 25 Jan 2008, 16:15:27 EST