Conformational ensemble of a multidomain protein explored by Gd³⁺ electron paramagnetic resonance.

ABSTRACT: Despite their importance in function, the conformational state of proteins and its changes are often poorly understood, mainly because of the lack of an efficient tool. MurD, a 47-kDa protein enzyme responsible for peptidoglycan biosynthesis, is one of those proteins whose conformational states and changes during their catalytic cycle are not well understood. Although it has been considered that MurD takes a single conformational state in solution as shown by a crystal structure, the solution nuclear magnetic resonance (NMR) study suggested the existence of multiple conformational state of apo MurD in solution. However, the conformational distribution has not been evaluated. In this work, we investigate the conformational states of MurD by the use of electron paramagnetic resonance (EPR),

SUBMITTER: Saio T 

PROVIDER: S-EPMC8391054 | biostudies-literature | 2021 Aug

REPOSITORIES: biostudies-literature