Periplasmic Binding Protein Dimer Has a Second Allosteric Event Tied to Ligand Binding
| Autor: | Le Li, Sarah L Lucas, Edward Wright, Dean A. A. Myles, Sudipa Ghimire-Rijal, Christopher B. Stanley, Matthew J. Cuneo, Pratul K. Agarwal |
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| Rok vydání: | 2017 |
| Předmět: |
Models
Molecular 0301 basic medicine Conformational change Stereochemistry Allosteric regulation ATP-binding cassette transporter Crystallography X-Ray Ligands Mannose-Binding Lectin Biochemistry 03 medical and health sciences Adenosine Triphosphate Protein structure Allosteric Regulation Bacterial Proteins ATP hydrolysis Thermotoga maritima Amino Acid Sequence Protein Structure Quaternary Chemistry Hydrolysis Binding protein Ligand (biochemistry) 030104 developmental biology Periplasmic Binding Proteins bacteria ATP-Binding Cassette Transporters Protein Multimerization Apoproteins Protein Binding |
| Zdroj: | Biochemistry. 56:5328-5337 |
| ISSN: | 1520-4995 0006-2960 |
| DOI: | 10.1021/acs.biochem.7b00657 |
| Popis: | 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 α-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. |
| Databáze: | OpenAIRE |
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