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Título: | Structural basis of a rationally rewired protein-protein interface critical to bacterial signaling |
Autor: | Podgornaia, Anna I.; Casino, Patricia CSIC ORCID; Marina, Alberto CSIC ORCID ; Laub, Michael T. | Fecha de publicación: | 2013 | Editor: | Elsevier | Citación: | Structure 21(9): 1636-1647 (2013) | Resumen: | Two-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. © 2013 Elsevier Ltd. | URI: | http://hdl.handle.net/10261/88244 | DOI: | 10.1016/j.str.2013.07.005 | Identificadores: | doi: 10.1016/j.str.2013.07.005 issn: 0969-2126 e-issn: 1878-4186 |
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