title: Variability and conservation of structural domains in divide-and-conquer approaches.
abstract: The use of protein building blocks for the structure determination of multidomain proteins and protein-protein complexes, also known as the "divide and conquer" approach, is an important strategy for obtaining protein structures. Atomic-resolution X-ray or NMR data of the individual domains are combined with lower-resolution electron microscopy maps or X-ray data of the full-length protein or the protein complex. Doing so, it is often assumed that the individual domain structures remain invariant in the context of the superstructure. In this work, we show the potentials and limitations of NMR to validate this approach at the example of the dodecameric DnaB helicase from Helicobacter pylori. We investigate how sequentially assigned spectra, as well as unassigned spectral fingerprints can be used to indicate the conservation of individual domains, and also to highlight conformational differences.
authors.affiliation: Physical Chemistry, ETH Zurich, 8093, Zurich, Switzerland.
authors.forename: Thomas
authors.initials: T
authors.lastname: Wiegand
authors.affiliation: Institut de Biologie et Chimie des Protéines, Bases Moléculaires et Structurales des Systèmes Infectieux, Labex Ecofect, UMR 5086 CNRS, Université de Lyon, 7 passage du Vercors, 69367, Lyon, France.|CRM2, UMR 7036, CNRS, Université de Lorraine, 54506, Vandoeuvre-lès-Nancy, France.
authors.forename: Carole
authors.initials: C
authors.lastname: Gardiennet
authors.affiliation: Physical Chemistry, ETH Zurich, 8093, Zurich, Switzerland.
authors.forename: Riccardo
authors.initials: R
authors.lastname: Cadalbert
authors.affiliation: Institut de Biologie et Chimie des Protéines, Bases Moléculaires et Structurales des Systèmes Infectieux, Labex Ecofect, UMR 5086 CNRS, Université de Lyon, 7 passage du Vercors, 69367, Lyon, France.
authors.forename: Denis
authors.initials: D
authors.lastname: Lacabanne
authors.affiliation: Institut de Biologie et Chimie des Protéines, Bases Moléculaires et Structurales des Systèmes Infectieux, Labex Ecofect, UMR 5086 CNRS, Université de Lyon, 7 passage du Vercors, 69367, Lyon, France.
authors.forename: Britta
authors.initials: B
authors.lastname: Kunert
authors.affiliation: Institut de Biologie et Chimie des Protéines, Bases Moléculaires et Structurales des Systèmes Infectieux, Labex Ecofect, UMR 5086 CNRS, Université de Lyon, 7 passage du Vercors, 69367, Lyon, France. laurent.terradot@ibcp.fr.
authors.forename: Laurent
authors.initials: L
authors.lastname: Terradot
authors.affiliation: Institut de Biologie et Chimie des Protéines, Bases Moléculaires et Structurales des Systèmes Infectieux, Labex Ecofect, UMR 5086 CNRS, Université de Lyon, 7 passage du Vercors, 69367, Lyon, France. a.bockmann@ibcp.fr.
authors.forename: Anja
authors.initials: A
authors.lastname: Böckmann
authors.affiliation: Physical Chemistry, ETH Zurich, 8093, Zurich, Switzerland. beme@ethz.ch.
authors.forename: Beat H
authors.initials: BH
authors.lastname: Meier
mesh_terms: D053488:DnaB Helicases / Q000737:chemistry; D019143:Evolution, Molecular; D014644:Genetic Variation; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D011487:Protein Conformation; D000072417:Protein Domains / Q000235:genetics; D011506:Proteins / Q000737:chemistry* / Q000235:genetics
chemical_list: D011506:Proteins; D053488:DnaB Helicases
keywords: DnaB; Domains; Protein; Solid-state NMR