Redox cofactors insertion in prokaryotic molybdoenzymes occurs via a conserved folding mechanism.

ABSTRACT: A major gap of knowledge in metalloproteins is the identity of the prefolded state of the protein before cofactor insertion. This holds for molybdoenzymes serving multiple purposes for life, especially in energy harvesting. This large group of prokaryotic enzymes allows for coordination of molybdenum or tungsten cofactors (Mo/W-bisPGD) and Fe/S clusters. Here we report the structural data on a cofactor-less enzyme, the nitrate reductase respiratory complex and characterize the conformational changes accompanying Mo/W-bisPGD and Fe/S cofactors insertion. Identified conformational changes are shown to be essential for recognition of the dedicated chaperone involved in cofactors insertion. A solvent-exposed salt bridge is shown to play a key role in enzyme folding after cofactors insertion. F

SUBMITTER: Arias-Cartin R 

PROVIDER: S-EPMC5123574 | biostudies-literature | 2016 Nov

REPOSITORIES: biostudies-literature