1y9u
From Proteopedia
(New page: 200px<br /><applet load="1y9u" size="450" color="white" frame="true" align="right" spinBox="true" caption="1y9u, resolution 1.39Å" /> '''Bordetella ferric bi...) |
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| - | [[Image:1y9u.gif|left|200px]]<br /><applet load="1y9u" size=" | + | [[Image:1y9u.gif|left|200px]]<br /><applet load="1y9u" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1y9u, resolution 1.39Å" /> | caption="1y9u, resolution 1.39Å" /> | ||
'''Bordetella ferric binding protein'''<br /> | '''Bordetella ferric binding protein'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Campylobacter jejuni, the leading cause of human gastroenteritis, expresses a ferric binding protein (cFbpA) that in many pathogenic | + | 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== | ==About this Structure== | ||
| - | 1Y9U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bordetella_pertussis_tohama_i Bordetella pertussis tohama i]. Full crystallographic information is available from [http:// | + | 1Y9U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bordetella_pertussis_tohama_i Bordetella pertussis tohama i]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y9U OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bordetella pertussis tohama i]] | [[Category: Bordetella pertussis tohama i]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bekker, E | + | [[Category: Bekker, E G.]] |
| - | [[Category: Cui, D | + | [[Category: Cui, D T.]] |
| - | [[Category: Murphy, M | + | [[Category: Murphy, M E.P.]] |
| - | [[Category: Tom-Yew, S | + | [[Category: Tom-Yew, S A.L.]] |
[[Category: iron tyrosinate interaction]] | [[Category: iron tyrosinate interaction]] | ||
[[Category: periplasmic binding protein]] | [[Category: periplasmic binding protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:03:14 2008'' |
Revision as of 14:03, 21 February 2008
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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
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