7oyw

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m (Protected "7oyw" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 7oyw is ON HOLD
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==E.coli's putrescine receptor variant PotF/D (4JDF) with mutations E39D F88L S247D in complex with spermidine==
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<StructureSection load='7oyw' size='340' side='right'caption='[[7oyw]], [[Resolution|resolution]] 1.28&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OYW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OYW FirstGlance]. <br>
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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]] 1.28&#8491;</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=3IE:(2~{S})-1-methoxypropan-2-amine'>3IE</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=JFN:(2R)-1-methoxypropan-2-amine'>JFN</scene>, <scene name='pdbligand=ONT:(2~{S})-1-(2-methoxyethoxy)propan-2-amine'>ONT</scene>, <scene name='pdbligand=ONW:(2~{R})-1-[(2~{R})-1-(2-methoxyethoxy)propan-2-yl]oxypropan-2-amine'>ONW</scene>, <scene name='pdbligand=SPD:SPERMIDINE'>SPD</scene></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=7oyw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7oyw OCA], [https://pdbe.org/7oyw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7oyw RCSB], [https://www.ebi.ac.uk/pdbsum/7oyw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7oyw ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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A profound understanding of the molecular interactions between receptors and ligands is important throughout diverse research such as protein design, drug discovery, or neuroscience. What determines specificity and how do proteins discriminate against similar ligands? In this study we analyzed factors that determine binding in two homologs belonging to the well-known superfamily of periplasmic binding proteins (PBPs), PotF and PotD. Building on a previously designed construct modes of polyamine binding were swapped. This change of specificity was approached by analyzing local differences in the binding pocket as well as overall conformational changes in the protein. Throughout the study, protein variants were generated and characterized structurally and thermodynamically, leading to a specificity swap and improvement in affinity. This dataset not only enriches our knowledge applicable to rational protein design, but our results can further lay groundwork for engineering of specific biosensors as well as help to explain the adaptability of pathogenic bacteria.
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Authors:
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Fine-tuning spermidine binding modes in the putrescine binding protein PotF.,Kroger P, Shanmugaratnam S, Scheib U, Hocker B J Biol Chem. 2021 Nov 18:101419. doi: 10.1016/j.jbc.2021.101419. PMID:34801550<ref>PMID:34801550</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 7oyw" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Hocker B]]
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[[Category: Kroeger P]]
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[[Category: Shanmugaratnam S]]

Current revision

E.coli's putrescine receptor variant PotF/D (4JDF) with mutations E39D F88L S247D in complex with spermidine

PDB ID 7oyw

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