View source for 5npo


==Promiscuous Protein Self-Assembly as a Function of Protein Stability==
<StructureSection load='5npo' size='340' side='right'caption='[[5npo]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5npo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NPO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NPO 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]] 1.95&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=5npo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5npo OCA], [https://pdbe.org/5npo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5npo RCSB], [https://www.ebi.ac.uk/pdbsum/5npo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5npo ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/D3INY1_ECOLX D3INY1_ECOLX] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Proteins have evolved to balance efficient binding of desired partners with rejection of unwanted interactions. To investigate the evolution of protein-protein interactions, we selected a random library of pre-stabilized TEM1 beta-lactamase against wild-type TEM1 using yeast surface display. Three mutations were sufficient to achieve micromolar affinity binding between the two. The X-ray structure emphasized that the main contribution of the selected mutations was to modify the protein fold, specifically removing the N'-terminal helix, which consequently allowed protein coupling via a beta-sheet-mediated interaction resembling amyloid interaction mode. The only selected mutation located at the interaction interface (E58V) is reminiscent of the single mutation commonly causing sickle-cell anemia. Interestingly, the evolved mutations cannot be inserted into the wild-type protein due to reduced thermal stability of the resulting mutant protein. These results reveal a simple mechanism by which undesirable binding is purged by loss of thermal stability.

Promiscuous Protein Binding as a Function of Protein Stability.,Cohen-Khait R, Dym O, Hamer-Rogotner S, Schreiber G Structure. 2017 Dec 5;25(12):1867-1874.e3. doi: 10.1016/j.str.2017.11.002. PMID:29211984<ref>PMID:29211984</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5npo" style="background-color:#fffaf0;"></div>

==See Also==
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Cohen-Khait R]]
[[Category: Dym O]]
[[Category: Hamer-Rogotner S]]
[[Category: Schreiber G]]