Faculty Collaboration Database

Two-state allosteric behavior in a single-domain signaling protein. Science 2001 Mar 23;291(5512):2429-33

Date

03/27/2001

Pubmed ID

11264542

DOI

10.1126/science.291.5512.2429

Scopus ID

2-s2.0-0035937443 (requires institutional sign-in at Scopus site)   541 Citations

Abstract

Protein actions are usually discussed in terms of static structures, but function requires motion. We find a strong correlation between phosphorylation-driven activation of the signaling protein NtrC and microsecond time-scale backbone dynamics. Using nuclear magnetic resonance relaxation, we characterized the motions of NtrC in three functional states: unphosphorylated (inactive), phosphorylated (active), and a partially active mutant. These dynamics are indicative of exchange between inactive and active conformations. Both states are populated in unphosphorylated NtrC, and phosphorylation shifts the equilibrium toward the active species. These results support a dynamic population shift between two preexisting conformations as the underlying mechanism of activation.

Author List

Volkman BF, Lipson D, Wemmer DE, Kern D

Author

Brian F. Volkman PhD Professor in the Biochemistry department at Medical College of Wisconsin

MESH terms used to index this publication - Major topics in bold

Allosteric Regulation
Bacterial Proteins
Binding Sites
DNA-Binding Proteins
Models, Molecular
Motion
Mutation
Nuclear Magnetic Resonance, Biomolecular
PII Nitrogen Regulatory Proteins
Phosphorylation
Protein Conformation
Protein Structure, Secondary
Protein Structure, Tertiary
Signal Transduction
Time
Trans-Activators
Transcription Factors