1mrp
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1mrp.jpg|left|200px]] | [[Image:1mrp.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1mrp", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | + | {{STRUCTURE_1mrp| PDB=1mrp | SCENE= }} | |
| - | | | + | |
| - | | | + | |
| - | }} | + | |
'''FERRIC-BINDING PROTEIN FROM HAEMOPHILUS INFLUENZAE''' | '''FERRIC-BINDING PROTEIN FROM HAEMOPHILUS INFLUENZAE''' | ||
| Line 32: | Line 29: | ||
[[Category: Nowalk, A J.]] | [[Category: Nowalk, A J.]] | ||
[[Category: Vaughan, K G.]] | [[Category: Vaughan, K G.]] | ||
| - | [[Category: | + | [[Category: Ferric iron binding protein]] |
| - | [[Category: | + | [[Category: Iron transport]] |
| - | [[Category: | + | [[Category: Periplasmic binding protein]] |
| - | [[Category: | + | [[Category: Transferrin superfamily]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:38:29 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 22:38, 2 May 2008
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. 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 Sat May 3 01:38:29 2008
