2m6k

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==Solution structure of the Escherichia coli apo ferric enterobactin binding protein==
==Solution structure of the Escherichia coli apo ferric enterobactin binding protein==
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<StructureSection load='2m6k' size='340' side='right'caption='[[2m6k]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''>
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<StructureSection load='2m6k' size='340' side='right'caption='[[2m6k]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2m6k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M6K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M6K FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2m6k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M6K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M6K FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2m6l|2m6l]]</div></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b0592, fepB, JW0584 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2m6k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m6k OCA], [https://pdbe.org/2m6k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m6k RCSB], [https://www.ebi.ac.uk/pdbsum/2m6k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m6k 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=2m6k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m6k OCA], [https://pdbe.org/2m6k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m6k RCSB], [https://www.ebi.ac.uk/pdbsum/2m6k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m6k ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/FEPB_ECOLI FEPB_ECOLI]] Binds ferrienterobactin; part of the binding-protein-dependent transport system for uptake of ferrienterobactin.
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[https://www.uniprot.org/uniprot/FEPB_ECOLI FEPB_ECOLI] Binds ferrienterobactin; part of the binding-protein-dependent transport system for uptake of ferrienterobactin.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The periplasmic binding protein (PBP) FepB plays a key role in transporting the catecholate siderophore ferric enterobactin from the outer to the inner membrane in Gram-negative bacteria. The solution structures of the 34-kDa apo- and holo-FepB from Escherichia coli, solved by NMR, represent the first solution structures determined for the type III class of PBPs. Unlike type I and II PBPs, which undergo large "Venus flytrap" conformational changes upon ligand binding, both forms of FepB maintain similar overall folds; however, binding of the ligand is accompanied by significant loop movements. Reverse methyl cross-saturation experiments corroborated chemical shift perturbation results and uniquely defined the binding pocket for gallium enterobactin (GaEnt). NMR relaxation experiments indicated that a flexible loop (residues 225-250) adopted a more rigid and extended conformation upon ligand binding, which positioned residues for optimal interactions with the ligand and the cytoplasmic membrane ABC transporter (FepCD), respectively. In conclusion, this work highlights the pivotal role that structural dynamics plays in ligand binding and transporter interactions in type III PBPs.
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The solution structure, binding properties, and dynamics of the bacterial siderophore-binding protein FepB.,Chu BC, Otten R, Krewulak KD, Mulder FA, Vogel HJ J Biol Chem. 2014 Oct 17;289(42):29219-34. doi: 10.1074/jbc.M114.564021. Epub, 2014 Aug 29. PMID:25173704<ref>PMID:25173704</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2m6k" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Ecoli]]
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[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Chu, B C.H]]
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[[Category: Chu BCH]]
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[[Category: Krewulak, K D]]
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[[Category: Krewulak KD]]
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[[Category: Mulder, F A.A]]
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[[Category: Mulder FAA]]
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[[Category: Otten, R]]
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[[Category: Otten R]]
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[[Category: Vogel, H J]]
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[[Category: Vogel HJ]]
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[[Category: Periplasmic]]
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[[Category: Siderophore]]
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[[Category: Transport protein]]
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Current revision

Solution structure of the Escherichia coli apo ferric enterobactin binding protein

PDB ID 2m6k

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