Periplasmic Binding Protein Dimer Has a Second Allosteric Event Tied to Ligand Binding

Li, Le; Ghimire-Rijal, Sudipa; Lucas, Sarah L.; Stanley, Christopher B.; Wright, Edward; Agarwal, Pratul K.; Myles, Dean A.; Cuneo, Matthew J.

doi:10.1021/acs.biochem.7b00657

Periplasmic Binding Protein Dimer Has a Second Allosteric Event Tied to Ligand Binding

Journal Article · Wed Sep 06 00:00:00 EDT 2017 · Biochemistry

DOI:https://doi.org/10.1021/acs.biochem.7b00657· OSTI ID:1407759

^[1]; Ghimire-Rijal, Sudipa ^[1]; Lucas, Sarah L. ^[2]; ^[1]; Wright, Edward ^[3]; ^[4]; Myles, Dean A. ^[1]; ^[1]

Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States); North Carolina State Univ., Raleigh, NC (United States)
Univ. of Tennessee, Knoxville, TN (United States)
Univ. of Tennessee, Knoxville, TN (United States); Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)

Here, the ligand-induced conformational changes of periplasmic binding proteins (PBP) play a key role in the acquisition of metabolites in ATP binding cassette (ABC) transport systems. This conformational change allows for differential recognition of the ligand occupancy of the PBP by the ABC transporter. This minimizes futile ATP hydrolysis in the transporter, a phenomenon in which ATP hydrolysis is not coupled to metabolite transport. In many systems, the PBP conformational change is insufficient at eliminating futile ATP hydrolysis. Here we identify an additional state of the PBP that is also allosterically regulated by the ligand. Ligand binding to the homodimeric apo PBP leads to a tightening of the interface alpha-helices so that the hydrogen bonding pattern shifts to that of a 3₁₀ helix, in-turn altering the contacts and the dynamics of the protein interface so that the monomer exists in the presence of ligand.

View Accepted Manuscript (DOE)

Research Organization:: Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)

Sponsoring Organization:: USDOE

Grant/Contract Number:: AC05-00OR22725

OSTI ID:: 1407759

Journal Information:: Biochemistry, Journal Name: Biochemistry Journal Issue: 40 Vol. 56; ISSN 0006-2960

Publisher:: American Chemical Society (ACS)Copyright Statement

Country of Publication:: United States

Language:: English

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