6v81

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Current revision (10:34, 23 October 2024) (edit) (undo)
 
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<StructureSection load='6v81' size='340' side='right'caption='[[6v81]], [[Resolution|resolution]] 2.96&Aring;' scene=''>
<StructureSection load='6v81' size='340' side='right'caption='[[6v81]], [[Resolution|resolution]] 2.96&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6v81]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_bw25113 Escherichia coli bw25113]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6V81 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6V81 FirstGlance]. <br>
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6V81 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6V81 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=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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]] 2.957&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">yncD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=679895 Escherichia coli BW25113])</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=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6v81 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6v81 OCA], [http://pdbe.org/6v81 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6v81 RCSB], [http://www.ebi.ac.uk/pdbsum/6v81 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6v81 ProSAT]</span></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=6v81 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6v81 OCA], [https://pdbe.org/6v81 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6v81 RCSB], [https://www.ebi.ac.uk/pdbsum/6v81 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6v81 ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
 
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[[http://www.uniprot.org/uniprot/YNCD_ECOLI YNCD_ECOLI]] Probable receptor, TonB-dependent.
 
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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The outer membrane of Gram-negative bacteria is highly impermeable to hydrophilic molecules of larger than 600 Da, protecting these bacteria from toxins present in the environment. In order to transport nutrients across this impermeable membrane, Gram-negative bacteria utilize a diverse family of outer-membrane proteins called TonB-dependent transporters. The majority of the members of this family transport iron-containing substrates. However, it is becoming increasingly clear that TonB-dependent transporters target chemically diverse substrates. In this work, the structure and phylogenetic distribution of the TonB-dependent transporter YncD are investigated. It is shown that while YncD is present in some enteropathogens, including Escherichia coli and Salmonella spp., it is also widespread in Gammaproteobacteria and Betaproteobacteria of environmental origin. The structure of YncD was determined, showing that despite a distant evolutionary relationship, it shares structural features with the ferric citrate transporter FecA, including a compact positively charged substrate-binding site. Despite these shared features, it is shown that YncD does not contribute to the growth of E. coli in pure culture under iron-limiting conditions or with ferric citrate as an iron source. Previous studies of transcriptional regulation in E. coli show that YncD is not induced under iron-limiting conditions and is unresponsive to the ferric uptake regulator (Fur). These observations, combined with the data presented here, suggest that YncD is not responsible for the transport of an iron-containing substrate.
 
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The crystal structure of the TonB-dependent transporter YncD reveals a positively charged substrate-binding site.,Grinter R, Lithgow T Acta Crystallogr D Struct Biol. 2020 May 1;76(Pt 5):484-495. doi:, 10.1107/S2059798320004398. Epub 2020 Apr 27. PMID:32355044<ref>PMID:32355044</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 6v81" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Escherichia coli bw25113]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Grinter, R]]
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[[Category: Grinter R]]
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[[Category: Gram-negative bacteria]]
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[[Category: Membrane protein]]
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[[Category: Outer membrane]]
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[[Category: Tonb-dependent transporter]]
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[[Category: Transport protein]]
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Current revision

The crystal structure of the outer-membrane transporter YncD

PDB ID 6v81

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