6yeb
From Proteopedia
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==E.coli's Putrescine receptor PotF in its closed apo state== | ==E.coli's Putrescine receptor PotF in its closed apo state== | ||
| - | <StructureSection load='6yeb' size='340' side='right'caption='[[6yeb]]' scene=''> | + | <StructureSection load='6yeb' size='340' side='right'caption='[[6yeb]], [[Resolution|resolution]] 1.97Å' 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=6YEB OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[6yeb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YEB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YEB FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[6ye0|6ye0]], [[6ye6|6ye6]], [[6ye7|6ye7]], [[6ye8|6ye8]]</div></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">potF, b0854, JW0838 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=6yeb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yeb OCA], [https://pdbe.org/6yeb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6yeb RCSB], [https://www.ebi.ac.uk/pdbsum/6yeb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6yeb ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/POTF_ECOLI POTF_ECOLI]] Required for the activity of the bacterial periplasmic transport system of putrescine. Polyamine binding protein. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Periplasmic binding proteins (PBPs) are ubiquitous receptors in gram-negative bacteria. They sense solutes and play key roles in nutrient uptake. Escherichia coli's putrescine receptor PotF has been reported to bind putrescine and spermidine. We reveal that several similar biogenic polyamines are recognized by PotF. Using isothermal titration calorimetry paired with X-ray crystallography of the different complexes, we unveil PotF's binding modes in detail. The binding site for PBPs is located between two lobes that undergo a large conformational change upon ligand recognition. Hence, analyzing the influence of ligands on complex formation is crucial. Therefore, we solved crystal structures of an open and closed apo state and used them as a basis for molecular dynamics simulations. In addition, we accessed structural behavior in solution for all complexes by (1)H-(15)N HSQC NMR spectroscopy. This combined analysis provides a robust framework for understanding ligand binding for future developments in drug design and protein engineering. | ||
| + | |||
| + | A comprehensive binding study illustrates ligand recognition in the periplasmic binding protein PotF.,Kroger P, Shanmugaratnam S, Ferruz N, Schweimer K, Hocker B Structure. 2020 Dec 30. pii: S0969-2126(20)30472-X. doi:, 10.1016/j.str.2020.12.005. PMID:33406388<ref>PMID:33406388</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6yeb" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Ecoli]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Hocker B]] | + | [[Category: Hocker, B]] |
| - | [[Category: Kroeger P]] | + | [[Category: Kroeger, P]] |
| - | [[Category: Shanmugaratnam S]] | + | [[Category: Shanmugaratnam, S]] |
| + | [[Category: Closed apo]] | ||
| + | [[Category: E coli]] | ||
| + | [[Category: Periplasmic binding protein]] | ||
| + | [[Category: Transport protein]] | ||
Revision as of 10:16, 19 May 2021
E.coli's Putrescine receptor PotF in its closed apo state
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