In-cell investigation of the conformational landscape of the GTPase UreG by SDSL-EPR.

ABSTRACT: UreG is a cytosolic GTPase involved in the maturation network of urease, an Ni-containing bacterial enzyme. Previous investigations in vitro showed that UreG features a flexible tertiary organization, making this protein the first enzyme discovered to be intrinsically disordered. To determine whether this heterogeneous behavior is maintained in the protein natural environment, UreG structural dynamics was investigated directly in intact bacteria by in-cell EPR. This approach, based on site-directed spin labeling coupled to electron paramagnetic resonance (SDSL-EPR) spectroscopy, enables the study of proteins in their native environment. The results show that UreG maintains heterogeneous structural landscape in-cell, existing in a conformational ensemble of two major co

SUBMITTER: Pierro A 

PROVIDER: S-EPMC10520941 | biostudies-literature | 2023 Oct

REPOSITORIES: biostudies-literature