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Article

The three-dimensional structure of two mutants of the signal transduction protein CheY suggest its molecular activation mechanism.

Journal of molecular biology - 22 Mar 1996

Bellsolell L, Cronet P, Majolero M, Serrano L, Coll M

Abstract excerpt

The three-dimensional crystal structures of the single mutant M17G and the triple mutant F14G-S15G-M17G of the response regulator protein CheY have been determined to 2.3 and 1.9 angstrom, respectively. Both mutants bind the essential Mg2+ cation as determined by the changes in stability, but binding does not cause the intrinsic fluorescence quenching of W58 observed in the wild-type protein. The loop...

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Identifiers

PMID: 8632450
DOI: 10.1006/jmbi.1996.0151

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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The three-dimensional structure of two mutants of the signal transduction protein CheY suggest its molecular activation mechanism.PMID 8632450Read ↗

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Genetic analysis of response regulator activation in bacterial chemotaxis suggests an intermolecular mechanism.Semantic proximity Read ↗

Structure analysis of two CheY mutants: importance of the hydrogen-bond contribution to protein stability.Semantic proximity Read ↗

Activation of the phosphosignaling protein CheY. II. Analysis of activated mutants by 19F NMR and protein engineering.Semantic proximity Read ↗

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The Solvation of the E. coli CheY Phosphorylation Site Mapped by XFMS.Semantic proximity Read ↗

Proposed signal transduction role for conserved CheY residue Thr87, a member of the response regulator active-site quintet.Semantic proximity Read ↗

Crystal structures of beryllium fluoride-free and beryllium fluoride-bound CheY in complex with the conserved C-terminal peptide of CheZ reveal dual binding modes specific to CheY conformation.Semantic proximity Read ↗

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