3p5n

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<StructureSection load='3p5n' size='340' side='right'caption='[[3p5n]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
<StructureSection load='3p5n' size='340' side='right'caption='[[3p5n]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3p5n]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staah Staah]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3P5N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3P5N FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3p5n]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_TCH60 Staphylococcus aureus subsp. aureus TCH60]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3P5N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3P5N FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=RBF:RIBOFLAVIN'>RBF</scene></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">X-ray diffraction, [[Resolution|Resolution]] 3.6&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HMPREF0772_2174 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=548473 STAAH])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=RBF:RIBOFLAVIN'>RBF</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=3p5n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p5n OCA], [https://pdbe.org/3p5n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3p5n RCSB], [https://www.ebi.ac.uk/pdbsum/3p5n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3p5n 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=3p5n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p5n OCA], [https://pdbe.org/3p5n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3p5n RCSB], [https://www.ebi.ac.uk/pdbsum/3p5n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3p5n ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/RIBU_STAAH RIBU_STAAH] Mediates riboflavin uptake, may also transport FMN and roseoflavin. Probably a riboflavin-binding protein that interacts with the energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates. The substrates themselves are bound by transmembrane, not extracytoplasmic soluble proteins (By similarity).
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The energy-coupling factor (ECF) transporters, responsible for vitamin uptake in prokaryotes, are a unique family of membrane transporters. Each ECF transporter contains a membrane-embedded, substrate-binding protein (known as the S component), an energy-coupling module that comprises two ATP-binding proteins (known as the A and A' components) and a transmembrane protein (known as the T component). The structure and transport mechanism of the ECF family remain unknown. Here we report the crystal structure of RibU, the S component of the ECF-type riboflavin transporter from Staphylococcus aureus at 3.6-A resolution. RibU contains six transmembrane segments, adopts a previously unreported transporter fold and contains a riboflavin molecule bound to the L1 loop and the periplasmic portion of transmembrane segments 4-6. Structural analysis reveals the essential ligand-binding residues, identifies the putative transport path and, with sequence alignment, uncovers conserved structural features and suggests potential mechanisms of action among the ECF transporters.
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Structure and mechanism of the S component of a bacterial ECF transporter.,Zhang P, Wang J, Shi Y Nature. 2010 Dec 2;468(7324):717-20. Epub 2010 Oct 24. PMID:20972419<ref>PMID:20972419</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 3p5n" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Staah]]
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[[Category: Staphylococcus aureus subsp. aureus TCH60]]
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[[Category: Shi, Y]]
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[[Category: Shi Y]]
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[[Category: Wang, J]]
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[[Category: Wang J]]
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[[Category: Zhang, P]]
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[[Category: Zhang P]]
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[[Category: Alpha-helical bundle]]
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[[Category: Transport protein]]
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[[Category: Transporter]]
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Current revision

Structure and mechanism of the S component of a bacterial ECF transporter

PDB ID 3p5n

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