Conformational Selection of Ubiquitin Quaternary Structures Driven by Zinc Ions. Issue 46 (10th October 2013)

• Record Type: Journal Article
• Authors: Fermani, Simona; Falini, Giuseppe; Calvaresi, Matteo; Bottoni, Andrea; Calò, Vincenza; Mangini, Vincenzo; Arnesano, Fabio; Natile, Giovanni
• Is Part Of: Chemistry. Volume 19:Issue 46(2013)
• Page Start: 15480
• Page End: 15484
• Publication Date: 2013-10-10
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1002/chem.201302229
• Languages: English
• ISSNs: 0947-6539

Abstract

<abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <bold>Zinc ions bridging two ubiquitin molecules</bold> (with His68 at the interface) contribute to select a subset of conformers from the noncovalent dimer ensemble, thus restricting quaternary structure dynamics, which hampers <italic>apo‐</italic>protein crystallization. The type of selected conformer is shown to determine the crystal packing, which varies from orthorhombic to cubic symmetry (see figure).<boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgg4t7pxgq6" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract>