1mrp
From Proteopedia
|
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 ... [(full description)]
About this Structure
1MRP is a [Single protein] structure of sequence from [Haemophilus influenzae] with FE and PO4 as [ligands]. Structure known Active Sites: FE and PO4. 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
Page seeded by OCA on Tue Oct 30 15:43:18 2007
