Contributions of Conformational Flexibility to High-Affinity Zinc Binding in the Solute Binding Protein AztC.

ABSTRACT: Bacteria rely on ATP binding cassette (ABC) transporters for the import of various nutrients. Bacterial ABC importers utilize an extracellular solute binding protein (SBP) to bind the substrate with high affinity and specificity and deliver it to the membrane permease for transport. The essential metals iron, manganese, and zinc are bound and transported by the cluster A-I SBPs. Crystal structures exist for the metal-bound and metal-free forms of several cluster A-I SBPs that show relatively subtle conformational changes that accompany metal binding. Recent solution studies and molecular dynamics simulations indicate a more complex conformational landscape for the cluster A-I SBPs, suggesting that changes in protein dynamics upon metal binding may have an important role in recognition by t

SUBMITTER: Serrano FA 

PROVIDER: S-EPMC8811889 | biostudies-literature | 2022 Feb

REPOSITORIES: biostudies-literature