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Structural basis of a rationally rewired protein-protein interface (HK853wt and RR468mutant V13P, L14I, I17M and N21V)Structural basis of a rationally rewired protein-protein interface (HK853wt and 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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