biostudies-literatureUnknown7(11)Lorenzi MMolecular recognition is central to all biological processes. Understanding the key role played by dedicated chaperones in metalloprotein folding and assembly requires the knowledge of their conformational ensembles. In this study, the NarJ chaperone dedicated to the assembly of the membrane-bound respiratory nitrate reductase complex NarGHI, a molybdenum-iron containing metalloprotein, was taken as a model of dedicated chaperone. The combination of two techniques ie site-directed spin labeling followed by EPR spectroscopy and ion mobility mass spectrometry, was used to get information about the structure and conformational dynamics of the NarJ chaperone upon binding the N-terminus of the NarG metalloprotein partner. By the study of singly spin-labeled proteins, the E119 residue present inPloS onee49523https://www.ebi.ac.uk/biostudies/studies/S-EPMC3501500biostudies-literatureConformational selection underlies recognition of a molybdoenzyme by its dedicated chaperone.PMC3501500Mileo EVezin HBelle VWalburger AHalgand FGerbaud GGuigliarelli BMagalon ASylvi LLorenzi MfalseConformational selection underlies recognition of a molybdoenzyme by its dedicated chaperone.Molecular recognition is central to all biological processes. Understanding the key role played by dedicated chaperones in metalloprotein folding and assembly requires the knowledge of their conformational ensembles. In this study, the NarJ chaperone dedicated to the assembly of the membrane-bound respiratory nitrate reductase complex NarGHI, a molybdenum-iron containing metalloprotein, was taken as a model of dedicated chaperone. The combination of two techniques ie site-directed spin labeling followed by EPR spectroscopy and ion mobility mass spectrometry, was used to get information about the structure and conformational dynamics of the NarJ chaperone upon binding the N-terminus of the NarG metalloprotein partner. By the study of singly spin-labeled proteins, the E119 residue present in2012-01-01T00:00:00Z20122026-05-02T09:20:07.763Z2019-03-26T23:19:10ZS-EPMC35015002318535010.1371/journal.pone.0049523