1qvs
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Crystal Structure of Haemophilus influenzae H9A mutant Holo Ferric ion-Binding Protein A
OverviewOverview
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 oxo-metal 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.
About this StructureAbout this Structure
1QVS is a Single protein structure of sequence from Haemophilus influenzae with FE and PO4 as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Presence of ferric hydroxide clusters in mutants of Haemophilus influenzae ferric ion-binding protein A., Shouldice SR, Skene RJ, Dougan DR, McRee DE, Tari LW, Schryvers AB, Biochemistry. 2003 Oct 21;42(41):11908-14. PMID:14556621
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