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Using Structural Information to Change the Phosphotransfer Specificity of a Two-Component Chemotaxis Signalling Complex
Author(s) -
Christian Bell,
Steven L. Porter,
Annabel Strawson,
David I. Stuart,
Judith P. Armitage
Publication year - 2010
Publication title -
plos biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.127
H-Index - 271
eISSN - 1545-7885
pISSN - 1544-9173
DOI - 10.1371/journal.pbio.1000306
Subject(s) - biology , chemotaxis , crosstalk , signal transduction , alanine scanning , histidine kinase , response regulator , histidine , biochemistry , microbiology and biotechnology , methionine , plasma protein binding , mutagenesis , receptor , amino acid , bacterial protein , mutation , physics , gene , optics
Analysis of the crystal structure of a phosphotransfer complex from the Rhodobacter sphaeroides chemotaxis pathway allowed reengineering of molecular recognition in a two-component signalling system.

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