1mrp
From Proteopedia
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FERRIC-BINDING PROTEIN FROM HAEMOPHILUS INFLUENZAE
Overview
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.
About this Structure
1MRP is a Single protein structure of sequence from Haemophilus influenzae with and as ligands. Known structural/functional Sites: and . Full crystallographic information is available from OCA.
Reference
Structure of Haemophilus influenzae Fe(+3)-binding protein reveals convergent evolution within a superfamily., Bruns CM, Nowalk AJ, Arvai AS, McTigue MA, Vaughan KG, Mietzner TA, McRee DE, Nat Struct Biol. 1997 Nov;4(11):919-24. PMID:9360608
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