title: Conformational selection of ubiquitin quaternary structures driven by zinc ions.
abstract: Zinc ions bridging two ubiquitin molecules (with His68 at the interface) contribute to select a subset of conformers from the noncovalent dimer ensemble, thus restricting quaternary structure dynamics, which hampers apo-protein crystallization. The type of selected conformer is shown to determine the crystal packing, which varies from orthorhombic to cubic symmetry.
authors.affiliation: Department of Chemistry "G. Ciamician", University of Bologna via F. Selmi 2, 40126 Bologna (Italy).
authors.forename: Simona
authors.initials: S
authors.lastname: Fermani
authors.forename: Giuseppe
authors.initials: G
authors.lastname: Falini
authors.forename: Matteo
authors.initials: M
authors.lastname: Calvaresi
authors.forename: Andrea
authors.initials: A
authors.lastname: Bottoni
authors.forename: Vincenza
authors.initials: V
authors.lastname: Calò
authors.forename: Vincenzo
authors.initials: V
authors.lastname: Mangini
authors.forename: Fabio
authors.initials: F
authors.lastname: Arnesano
authors.forename: Giovanni
authors.initials: G
authors.lastname: Natile
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D007477:Ions / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D011487:Protein Conformation; D054730:Protein Interaction Domains and Motifs; D025801:Ubiquitin / Q000737:chemistry*; D014961:X-Ray Diffraction; D015032:Zinc / Q000737:chemistry*
chemical_list: D007477:Ions; D025801:Ubiquitin; D015032:Zinc
keywords: NMR spectroscopy; X-ray diffraction; protein-protein interactions; ubiquitin; zinc