1y9u: Difference between revisions
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< | ==Bordetella ferric binding protein== | ||
<StructureSection load='1y9u' size='340' side='right'caption='[[1y9u]], [[Resolution|resolution]] 1.39Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1y9u]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y9U FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.39Å</td></tr> | |||
-- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1y9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y9u OCA], [https://pdbe.org/1y9u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y9u RCSB], [https://www.ebi.ac.uk/pdbsum/1y9u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y9u ProSAT]</span></td></tr> | ||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q7VXW9_BORPE Q7VXW9_BORPE] | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/y9/1y9u_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1y9u ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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<ref>PMID:15613474</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1y9u" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Ferric-binding protein|Ferric-binding protein]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Bordetella pertussis Tohama I]] | ||
[[Category: Large Structures]] | |||
[[Category: Bekker EG]] | |||
== | [[Category: Cui DT]] | ||
[[Category: Murphy MEP]] | |||
[[Category: Bordetella pertussis | [[Category: Tom-Yew SAL]] | ||
[[Category: | |||
[[Category: Bekker | |||
[[Category: Cui | |||
[[Category: Murphy | |||
[[Category: Tom-Yew | |||
Latest revision as of 10:41, 30 October 2024
Bordetella ferric binding proteinBordetella ferric binding protein
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCampylobacter 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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