1y4t
From Proteopedia
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|PDB= 1y4t |SIZE=350|CAPTION= <scene name='initialview01'>1y4t</scene>, resolution 1.80Å | |PDB= 1y4t |SIZE=350|CAPTION= <scene name='initialview01'>1y4t</scene>, resolution 1.80Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=FE:FE (III) ION'>FE</scene> | + | |LIGAND= <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1y4t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y4t OCA], [http://www.ebi.ac.uk/pdbsum/1y4t PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1y4t RCSB]</span> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Murphy, M E.P.]] | [[Category: Murphy, M E.P.]] | ||
[[Category: Tom-Yew, S A.L.]] | [[Category: Tom-Yew, S A.L.]] | ||
| - | [[Category: FE]] | ||
[[Category: iron-tyrosinate]] | [[Category: iron-tyrosinate]] | ||
[[Category: periplasmic binding protein]] | [[Category: periplasmic binding protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:58:47 2008'' |
Revision as of 21:58, 30 March 2008
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| , resolution 1.80Å | |||||||
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Ferric binding protein from Campylobacter jejuni
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
1Y4T is a Single protein structure of sequence from Campylobacter jejuni. 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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