7r7b
From Proteopedia
(Difference between revisions)
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==1.50 Angstroem Crystal Structure of FeoA from Bacteroides fragilis== | ==1.50 Angstroem Crystal Structure of FeoA from Bacteroides fragilis== | ||
| - | <StructureSection load='7r7b' size='340' side='right'caption='[[7r7b]]' scene=''> | + | <StructureSection load='7r7b' size='340' side='right'caption='[[7r7b]], [[Resolution|resolution]] 1.50Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7R7B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7R7B FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7r7b]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteroides_fragilis Bacteroides fragilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7R7B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7R7B FirstGlance]. <br> |
| - | </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=7r7b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7r7b OCA], [https://pdbe.org/7r7b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7r7b RCSB], [https://www.ebi.ac.uk/pdbsum/7r7b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7r7b ProSAT]</span></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]] 1.5Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=7r7b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7r7b OCA], [https://pdbe.org/7r7b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7r7b RCSB], [https://www.ebi.ac.uk/pdbsum/7r7b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7r7b ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q5LFM5_BACFN Q5LFM5_BACFN] Probable transporter of a GTP-driven Fe(2+) uptake system.[RuleBase:RU362098] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Iron is an essential element for nearly all organisms, and under anoxic and/or reducing conditions, Fe(2+) is the dominant form of iron available to bacteria. The ferrous iron transport (Feo) system is the primary prokaryotic Fe(2+) import machinery, and two constituent proteins (FeoA and FeoB) are conserved across most bacterial species. However, how FeoA and FeoB function relative to one another remains enigmatic. In this work, we explored the distribution of feoAB operons encoding a fusion of FeoA tethered to the N-terminal, G-protein domain of FeoB via a connecting linker region. We hypothesized that this fusion poises FeoA to interact with FeoB to affect function. To test this hypothesis, we characterized the soluble NFeoAB fusion protein from Bacteroides fragilis, a commensal organism implicated in drug-resistant infections. Using X-ray crystallography, we determined the 1.50-A resolution structure of BfFeoA, which adopts an SH3-like fold implicated in protein-protein interactions. Using a combination of structural modeling, small-angle X-ray scattering, and hydrogen-deuterium exchange mass spectrometry, we show that FeoA and NFeoB interact in a nucleotide-dependent manner, and we mapped the protein-protein interaction interface. Finally, using guanosine triphosphate (GTP) hydrolysis assays, we demonstrate that BfNFeoAB exhibits one of the slowest known rates of Feo-mediated GTP hydrolysis that is not potassium-stimulated. Importantly, truncation of FeoA from this fusion demonstrates that FeoA-NFeoB interactions function to stabilize the GTP-bound form of FeoB. Taken together, our work reveals a role for FeoA function in the fused FeoAB system and suggests a function for FeoA among prokaryotes. | ||
| + | |||
| + | A fusion of the Bacteroides fragilis ferrous iron import proteins reveals a role for FeoA in stabilizing GTP-bound FeoB.,Sestok AE, Brown JB, Obi JO, O'Sullivan SM, Garcin ED, Deredge DJ, Smith AT J Biol Chem. 2022 Apr;298(4):101808. doi: 10.1016/j.jbc.2022.101808. Epub 2022, Mar 8. PMID:35271852<ref>PMID:35271852</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7r7b" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Bacteroides fragilis]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Sestok AE]] | [[Category: Sestok AE]] | ||
[[Category: Smith AT]] | [[Category: Smith AT]] | ||
Current revision
1.50 Angstroem Crystal Structure of FeoA from Bacteroides fragilis
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