Presence of ferric hydroxide clusters in mutants of Haemophilus influenzae ferric ion-binding protein A

Shouldice, Stephen R., Skene, Robert J., Dougan, Douglas R., McRee, Duncan E., Tari, Leslie W. and Schryvers, Anthony B. (2003) Presence of ferric hydroxide clusters in mutants of Haemophilus influenzae ferric ion-binding protein A. Biochemistry, 42 41: 11908-11914. doi:10.1021/bi035389s


Author Shouldice, Stephen R.
Skene, Robert J.
Dougan, Douglas R.
McRee, Duncan E.
Tari, Leslie W.
Schryvers, Anthony B.
Title Presence of ferric hydroxide clusters in mutants of Haemophilus influenzae ferric ion-binding protein A
Journal name Biochemistry   Check publisher's open access policy
ISSN 0006-2960
Publication date 2003-01-01
Sub-type Article (original research)
DOI 10.1021/bi035389s
Open Access Status Not Open Access
Volume 42
Issue 41
Start page 11908
End page 11914
Total pages 7
Place of publication Washington D.C., USA
Publisher American Chemical Society
Language eng
Subject 0601 Biochemistry and Cell Biology
Abstract The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. In this study, we report the crystal structures of two mutant forms of ferric ion-binding protein A (FbpA) from Haemophilus influenzae with bound multinuclear oxometal clusters. Crystals of site-directed mutants in the metal or anion binding ligands contain protein in the open conformation, and two mutant FbpAs, H9A and N175L, contain different cluster arrangements in the iron-binding pocket. The iron clusters are anchored by binding to the two tyrosine ligands (Tyr195 and Tyr196) positioned at the vertex of the iron-binding pocket but are not coordinated by the other metal binding ligands. Our results suggest that the metal clusters may have formed in situ, suggesting that the mutant FbpAs may serve as a simple model for protein-mediated mineralization.
Keyword Biochemistry & Molecular Biology
Human Serum Transferrin
Terminal Half-molecule
Induced Conformational Change
Crystal-structure
Iron-binding
N-lobe
Bacterial Transferrin
Pathogenic Neisseria
Human Lactoferrin
Escherichia-coli
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: Sat, 26 Jan 2008, 02:02:19 EST