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PDBsum entry 4jav
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Transferase/signaling protein
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PDB id
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4jav
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References listed in PDB file
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Key reference
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Title
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Structural basis of a rationally rewired protein-Protein interface critical to bacterial signaling.
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Authors
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A.I.Podgornaia,
P.Casino,
A.Marina,
M.T.Laub.
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Ref.
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Structure, 2013,
21,
1636-1647.
[DOI no: ]
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PubMed id
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Abstract
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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.
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