1efd: Difference between revisions
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<StructureSection load='1efd' size='340' side='right' caption='[[1efd]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='1efd' size='340' side='right' caption='[[1efd]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1efd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1efd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EFD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EFD FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GCR:GALLICHROME'>GCR</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GCR:GALLICHROME'>GCR</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1efd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1efd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1efd RCSB], [http://www.ebi.ac.uk/pdbsum/1efd PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1efd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1efd OCA], [http://pdbe.org/1efd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1efd RCSB], [http://www.ebi.ac.uk/pdbsum/1efd PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1efd" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bacillus coli migula 1895]] | ||
[[Category: Clarke, T E]] | [[Category: Clarke, T E]] | ||
[[Category: Dougan, D R]] | [[Category: Dougan, D R]] | ||
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[[Category: Tari, L W]] | [[Category: Tari, L W]] | ||
[[Category: Vogel, H J]] | [[Category: Vogel, H J]] | ||
[[Category: Escherichia coli]] | |||
[[Category: Ferric siderophore binding protein]] | [[Category: Ferric siderophore binding protein]] | ||
[[Category: Fhud complex with gallichrome]] | [[Category: Fhud complex with gallichrome]] | ||
[[Category: Metal transport]] | [[Category: Metal transport]] | ||
[[Category: Periplasmic binding protein-siderophore complex]] | [[Category: Periplasmic binding protein-siderophore complex]] | ||
Revision as of 20:45, 11 September 2015
PERIPLASMIC FERRIC SIDEROPHORE BINDING PROTEIN FHUD COMPLEXED WITH GALLICHROMEPERIPLASMIC FERRIC SIDEROPHORE BINDING PROTEIN FHUD COMPLEXED WITH GALLICHROME
Structural highlights
Function[FHUD_ECOLI] Part of the ABC transporter complex FhuCDB involved in iron(3+)-hydroxamate import. Binds the iron(3+)-hydroxamate complex and transfers it to the membrane-bound permease. Required for the transport of all iron(3+)-hydroxamate siderophores such as ferrichrome, gallichrome, desferrioxamine, coprogen, aerobactin, shizokinen, rhodotorulic acid and the antibiotic albomycin. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedSiderophore binding proteins play a key role in the uptake of iron in many gram-positive and gram-negative bacteria. FhuD is a soluble periplasmic binding protein that transports ferrichrome and other hydroxamate siderophores. The crystal structure of FhuD from Escherichia coli in complex with the ferrichrome homolog gallichrome has been determined at 1.9 inverted question mark resolution, the first structure of a periplasmic binding protein involved in the uptake of siderophores. Gallichrome is held in a shallow pocket lined with aromatic groups; Arg and Tyr side chains interact directly with the hydroxamate moieties of the siderophore. FhuD possesses a novel fold, suggesting that its mechanisms of ligand binding and release are different from other structurally characterized periplasmic ligand binding proteins. The structure of the ferric siderophore binding protein FhuD complexed with gallichrome.,Clarke TE, Ku SY, Dougan DR, Vogel HJ, Tari LW Nat Struct Biol. 2000 Apr;7(4):287-91. PMID:10742172[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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