1QVS

Crystal Structure of Haemophilus influenzae H9A mutant Holo Ferric ion-Binding Protein A

Summary for 1QVS

• Entry DOI: 10.2210/pdb1qvs/pdb
• Descriptor: Iron-utilization periplasmic protein, FE (III) ION, PHOSPHATE ION, ... (4 entities in total)
• Functional Keywords: metal binding protein
• Biological source: Haemophilus influenzae
• Cellular location: Periplasm (Probable): P35755
• Total number of polymer chains: 1
• Total formula weight: 34059.66

Authors

Shouldice, S.R.,Skene, R.J.,Dougan, D.R.,McRee, D.E.,Tari, L.W.,Schryvers, A.B. (deposition date: 2003-08-28, release date: 2003-11-04, Last modification date: 2023-08-16)

Primary citation

Shouldice, S.R.,Skene, R.J.,Dougan, D.R.,McRee, D.E.,Tari, L.W.,Schryvers, A.B.
Presence of ferric hydroxide clusters in mutants of Haemophilus influenzae ferric ion-binding protein A
Biochemistry, 42:11908-11914, 2003

PubMed 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 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.

PubMed: 14556621
DOI: 10.1021/bi035389s

Experimental method

X-RAY DIFFRACTION (2.1 Å)