4ja2: Difference between revisions
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==Structural basis of a rationally rewired protein-protein interface (RR468mutant V13P, L14I, I17M and N21V)== | ==Structural basis of a rationally rewired protein-protein interface (RR468mutant V13P, L14I, I17M and N21V)== | ||
<StructureSection load='4ja2' size='340' side='right' caption='[[4ja2]], [[Resolution|resolution]] 1.79Å' scene=''> | <StructureSection load='4ja2' size='340' side='right'caption='[[4ja2]], [[Resolution|resolution]] 1.79Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ja2]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4ja2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JA2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JA2 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand= | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BFD:ASPARTATE+BERYLLIUM+TRIFLUORIDE'>BFD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4ja2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ja2 OCA], [https://pdbe.org/4ja2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ja2 RCSB], [https://www.ebi.ac.uk/pdbsum/4ja2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ja2 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9WYT9_THEMA Q9WYT9_THEMA] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[Response regulator|Response regulator]] | *[[Response regulator 3D structure|Response regulator 3D structure]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Thermotoga maritima MSB8]] | ||
[[Category: | [[Category: Casino P]] | ||
[[Category: | [[Category: Laub MT]] | ||
[[Category: | [[Category: Marina A]] | ||
[[Category: | [[Category: Podgornaia AI]] | ||
Revision as of 14:01, 24 November 2022
Structural basis of a rationally rewired protein-protein interface (RR468mutant V13P, L14I, I17M and N21V)Structural basis of a rationally rewired protein-protein interface (RR468mutant V13P, L14I, I17M and N21V)
Structural highlights
FunctionPublication Abstract from PubMedTwo-component signal transduction systems typically involve a sensor histidine kinase that specifically phosphorylates a single, cognate response regulator. This protein-protein interaction relies on molecular recognition via a small set of residues in each protein. To better understand how these residues determine the specificity of kinase-substrate interactions, we rationally rewired the interaction interface of a Thermotoga maritima two-component system, HK853-RR468, to match that found in a different two-component system, Escherichia coli PhoR-PhoB. The rewired proteins interacted robustly with each other, but no longer interacted with the parent proteins. Analysis of the crystal structures of the wild-type and mutant protein complexes and a systematic mutagenesis study reveal how individual mutations contribute to the rewiring of interaction specificity. Our approach and conclusions have implications for studies of other protein-protein interactions and protein evolution and for the design of novel protein interfaces. Structural Basis of a Rationally Rewired Protein-Protein Interface Critical to Bacterial Signaling.,Podgornaia AI, Casino P, Marina A, Laub MT Structure. 2013 Aug 13. pii: S0969-2126(13)00254-2. doi:, 10.1016/j.str.2013.07.005. PMID:23954504[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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