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Structural heterogeneity in microcrystalline ubiquitin studied by solid-state NMR.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Becker, Stefan Loquet, Antoine Giller, Karin Wolff, Sebastian Fasshuber, Hannes Klaus Lakomek, Nils-Alexander Lange, Adam Shi, Chaowei Habenstein, Birgit
Description	Country affiliation: Germany Author Affiliation: Fasshuber HK ( Department of NMR-Based Structural Biology, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany)
Abstract	By applying [1-(13) C]- and [2-(13) C]-glucose labeling schemes to the folded globular protein ubiquitin, a strong reduction of spectral crowding and increase in resolution in solid-state NMR (ssNMR) spectra could be achieved. This allowed spectral resonance assignment in a straightforward manner and the collection of a wealth of long-range distance information. A high precision solid-state NMR structure of microcrystalline ubiquitin was calculated with a backbone rmsd of 1.57 to the X-ray structure and 1.32 Å to the solution NMR structure. Interestingly, we can resolve structural heterogeneity as the presence of three slightly different conformations. Structural heterogeneity is most significant for the loop region ß1-ß2 but also for ß-strands ß1, ß2, ß3, and ß5 as well as for the loop connecting 1 and ß3. This structural polymorphism observed in the solid-state NMR spectra coincides with regions that showed dynamics in solution NMR experiments on different timescales.
ISSN	09618368
e-ISSN	1469896X
DOI	10.1002/pro.2654
Journal	Protein Science
Issue Number	5
Volume Number	24
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2015-05-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Nuclear Magnetic Resonance, Biomolecular Protein Structure, Secondary Ubiquitin Chemistry Crystallography, X-ray Models, Molecular Protein Folding Research Support, Non-u.s. Gov't Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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