1y9u
From Proteopedia
Line 1: | Line 1: | ||
[[Image:1y9u.gif|left|200px]] | [[Image:1y9u.gif|left|200px]] | ||
- | + | <!-- | |
- | + | The line below this paragraph, containing "STRUCTURE_1y9u", 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_1y9u| PDB=1y9u | SCENE= }} | |
- | + | ||
- | + | ||
- | }} | + | |
'''Bordetella ferric binding protein''' | '''Bordetella ferric binding protein''' | ||
Line 29: | Line 26: | ||
[[Category: Murphy, M E.P.]] | [[Category: Murphy, M E.P.]] | ||
[[Category: Tom-Yew, S A.L.]] | [[Category: Tom-Yew, S A.L.]] | ||
- | [[Category: | + | [[Category: Iron tyrosinate interaction]] |
- | [[Category: | + | [[Category: Periplasmic binding protein]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:03:24 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 13:03, 3 May 2008
Bordetella ferric binding protein
Overview
Campylobacter jejuni, the leading cause of human gastroenteritis, expresses a ferric binding protein (cFbpA) that in many pathogenic bacteria functions to acquire iron as part of their virulence repertoire. Recombinant cFbpA is isolated with ferric iron bound from Escherichia coli. The crystal structure of cFbpA reveals unprecedented iron coordination by only five protein ligands. The histidine and one tyrosine are derived from the N-terminal domain, whereas the three remaining tyrosine ligands are from the C-terminal domain. Surprisingly, a synergistic anion present in all other characterized ferric transport proteins is not observed in the cFbpA iron-binding site, suggesting a novel role for this protein in iron uptake. Furthermore, cFbpA is shown to bind iron with high affinity similar to Neisserial FbpA and exhibits an unusual preference for ferrous iron (oxidized subsequently to the ferric form) or ferric iron chelated by oxalate. Sequence and structure analyses reveal that cFbpA is a member of a new class of ferric binding proteins that includes homologs from invasive and intracellular bacteria as well as cyanobacteria. Overall, six classes are defined based on clustering within the tree and by their putative iron coordination. The absence of a synergistic anion in the iron coordination sphere of cFbpA also suggests an alternative model of evolution for FbpA homologs involving an early iron-binding ancestor instead of a requirement for a preexisting anion-binding ancestor.
About this Structure
1Y9U is a Single protein structure of sequence from Bordetella pertussis tohama i. Full crystallographic information is available from OCA.
Reference
Anion-independent iron coordination by the Campylobacter jejuni ferric binding protein., Tom-Yew SA, Cui DT, Bekker EG, Murphy ME, J Biol Chem. 2005 Mar 11;280(10):9283-90. Epub 2004 Dec 21. PMID:15613474 Page seeded by OCA on Sat May 3 16:03:24 2008