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| | <StructureSection load='5uy4' size='340' side='right'caption='[[5uy4]], [[Resolution|resolution]] 1.92Å' scene=''> | | <StructureSection load='5uy4' size='340' side='right'caption='[[5uy4]], [[Resolution|resolution]] 1.92Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5uy4]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UY4 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5UY4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5uy4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Yersinia_pestis Yersinia pestis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UY4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UY4 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.915Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5uxs|5uxs]], [[5uxu|5uxu]], [[5uy0|5uy0]], [[5uy5|5uy5]], [[5uya|5uya]], [[5uyb|5uyb]], [[5uyd|5uyd]], [[5uye|5uye]], [[5uyf|5uyf]], [[5uyg|5uyg]], [[5uyh|5uyh]], [[5uyc|5uyc]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5uy4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uy4 OCA], [http://pdbe.org/5uy4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5uy4 RCSB], [http://www.ebi.ac.uk/pdbsum/5uy4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5uy4 ProSAT]</span></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=5uy4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uy4 OCA], [https://pdbe.org/5uy4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5uy4 RCSB], [https://www.ebi.ac.uk/pdbsum/5uy4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5uy4 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/YFEA_YERPE YFEA_YERPE]] Part of an ATP-driven transport system YfeABCD for chelated iron. | + | [https://www.uniprot.org/uniprot/YFEA_YERPE YFEA_YERPE] Part of an ATP-driven transport system YfeABCD for chelated iron. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Aller, S G]] | + | [[Category: Yersinia pestis]] |
| - | [[Category: DeLucas, L J]] | + | [[Category: Aller SG]] |
| - | [[Category: Radka, C D]] | + | [[Category: DeLucas LJ]] |
| - | [[Category: Metal transport]] | + | [[Category: Radka CD]] |
| - | [[Category: Polyspecific]]
| + | |
| - | [[Category: Transition metal]]
| + | |
| - | [[Category: Transport]]
| + | |
| Structural highlights
Function
YFEA_YERPE Part of an ATP-driven transport system YfeABCD for chelated iron.
Publication Abstract from PubMed
Gram-negative bacteria use siderophores, outer membrane receptors, inner membrane transporters and substrate-binding proteins (SBPs) to transport transition metals through the periplasm. The SBPs share a similar protein fold that has undergone significant structural evolution to communicate with a variety of differentially regulated transporters in the cell. In Yersinia pestis, the causative agent of plague, YfeA (YPO2439, y1897), an SBP, is important for full virulence during mammalian infection. To better understand the role of YfeA in infection, crystal structures were determined under several environmental conditions with respect to transition-metal levels. Energy-dispersive X-ray spectroscopy and anomalous X-ray scattering data show that YfeA is polyspecific and can alter its substrate specificity. In minimal-media experiments, YfeA crystals grown after iron supplementation showed a threefold increase in iron fluorescence emission over the iron fluorescence emission from YfeA crystals grown from nutrient-rich conditions, and YfeA crystals grown after manganese supplementation during overexpression showed a fivefold increase in manganese fluorescence emission over the manganese fluorescence emission from YfeA crystals grown from nutrient-rich conditions. In all experiments, the YfeA crystals produced the strongest fluorescence emission from zinc and could not be manipulated otherwise. Additionally, this report documents the discovery of a novel surface metal-binding site that prefers to chelate zinc but can also bind manganese. Flexibility across YfeA crystal forms in three loops and a helix near the buried metal-binding site suggest that a structural rearrangement is required for metal loading and unloading.
Crystal structure of Yersinia pestis virulence factor YfeA reveals two polyspecific metal-binding sites.,Radka CD, DeLucas LJ, Wilson LS, Lawrenz MB, Perry RD, Aller SG Acta Crystallogr D Struct Biol. 2017 Jul 1;73(Pt 7):557-572. doi:, 10.1107/S2059798317006349. Epub 2017 Jun 30. PMID:28695856[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Radka CD, DeLucas LJ, Wilson LS, Lawrenz MB, Perry RD, Aller SG. Crystal structure of Yersinia pestis virulence factor YfeA reveals two polyspecific metal-binding sites. Acta Crystallogr D Struct Biol. 2017 Jul 1;73(Pt 7):557-572. doi:, 10.1107/S2059798317006349. Epub 2017 Jun 30. PMID:28695856 doi:http://dx.doi.org/10.1107/S2059798317006349
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