1mrp
From Proteopedia
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==Overview== | ==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 ... | + | 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== | ==About this Structure== | ||
| - | 1MRP is a | + | 1MRP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae] with FE and PO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Sites: FE and PO4. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MRP OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transferrin superfamily]] | [[Category: transferrin superfamily]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 13:09:37 2007'' |
Revision as of 11:04, 5 November 2007
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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 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
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