View source for 7oyx


==E.coli's putrescine receptor variant PotF/D (4JDF) with mutations E39D Y87S F88Y S247D in complex with spermidine==
<StructureSection load='7oyx' size='340' side='right'caption='[[7oyx]], [[Resolution|resolution]] 1.37&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OYX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OYX FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.37&#8491;</td></tr>
<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=3IK:(2~{R})-1-[(2~{R})-1-[(2~{S})-1-[(2~{S})-1-(2-methoxyethoxy)propan-2-yl]oxypropan-2-yl]oxypropan-2-yl]oxypropan-2-amine'>3IK</scene>, <scene name='pdbligand=4RH:(2~{R})-1-(2-methoxyethoxy)propan-2-amine'>4RH</scene>, <scene name='pdbligand=4SW:(2~{S})-1-[(2~{R})-1-(2-methoxyethoxy)propan-2-yl]oxypropan-2-amine'>4SW</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ONT:(2~{S})-1-(2-methoxyethoxy)propan-2-amine'>ONT</scene>, <scene name='pdbligand=SPD:SPERMIDINE'>SPD</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=7oyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7oyx OCA], [https://pdbe.org/7oyx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7oyx RCSB], [https://www.ebi.ac.uk/pdbsum/7oyx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7oyx ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7oyx" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Hocker B]]
[[Category: Kroeger P]]
[[Category: Shanmugaratnam S]]