1MRP

FERRIC-BINDING PROTEIN FROM HAEMOPHILUS INFLUENZAE

Summary for 1MRP

• Entry DOI: 10.2210/pdb1mrp/pdb
• Descriptor: FERRIC IRON BINDING PROTEIN, FE (III) ION, PHOSPHATE ION, ... (4 entities in total)
• Functional Keywords: ferric iron binding protein, periplasmic binding protein, iron transport, transferrin superfamily
• Biological source: Haemophilus influenzae
• Cellular location: Periplasm (Probable): P35755
• Total number of polymer chains: 1
• Total formula weight: 33920.07

Authors

Bruns, C.M.,Nowalk, A.J.,Arvai, A.S.,Mctigue, M.A.,Vaughan, K.G.,Mietzner, T.A.,Mcree, D.E. (deposition date: 1997-05-14, release date: 1998-01-28, Last modification date: 2024-02-14)

Primary citation

Bruns, C.M.,Nowalk, A.J.,Arvai, A.S.,McTigue, M.A.,Vaughan, K.G.,Mietzner, T.A.,McRee, D.E.
Structure of Haemophilus influenzae Fe(+3)-binding protein reveals convergent evolution within a superfamily.
Nat.Struct.Biol., 4:919-924, 1997

PubMed Abstract: The first crystal structure of the iron-transporter ferric ion-binding protein from Haemophilus influenzae (hFBP), at 1.6 A resolution, reveals the structural basis for iron uptake and transport required by several important bacterial pathogens. Paradoxically, although hFBP belongs to a protein superfamily which includes human transferrin, iron binding in hFBP and transferrin appears to have developed independently by convergent evolution. Structural comparison of hFBP with other prokaryotic periplasmic transport proteins and the eukaryotic transferrins suggests that these proteins are related by divergent evolution from an anion-binding common ancestor, not from an iron-binding ancestor. The iron binding site of hFBP incorporates a water and an exogenous phosphate ion as iron ligands and exhibits nearly ideal octahedral metal coordination. FBP is highly conserved, required for virulence, and is a nodal point for free iron uptake in several Gram-negative pathogenic bacteria, thus providing a potential target for broad-spectrum antibacterial drug design against human pathogens such as H. influenzae, Neisseria gonorrhoeae, and Neisseria meningitidis.

PubMed: 9360608
DOI: 10.1038/nsb1197-919

Experimental method

X-RAY DIFFRACTION (1.6 Å)