Solution NMR evidence for symmetry in functionally or crystallographically asymmetric homodimers.

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TitleSolution NMR evidence for symmetry in functionally or crystallographically asymmetric homodimers.
Publication TypeJournal Article
Year of Publication2011
AuthorsGodoy-Ruiz, R, Krejcirikova, A, D Gallagher, T, Tugarinov, V
JournalJ Am Chem Soc
Volume133
Issue49
Pagination19578-81
Date Published2011 Dec 14
ISSN1520-5126
KeywordsBacterial Proteins, Crystallography, X-Ray, Cyclic AMP Receptor Protein, Geobacillus stearothermophilus, Models, Molecular, Mycobacterium tuberculosis, Nuclear Magnetic Resonance, Biomolecular, Protein Conformation, Protein Multimerization
Abstract

A recurrent theme of many structural studies of homo-oligomeric protein systems is concerned with verification that the conformation observed in a crystal represents the functionally relevant structure. An asymmetric conformation adopted by two chemically identical subunits in homo-oligomers can represent an intrinsic property of a protein or be an artifact induced by crystal packing forces. Solution NMR studies can distinguish between these two possibilities. Using methyl-based NMR spectroscopy, we provide evidence for symmetry in the absence of ligands in several homodimeric proteins that are either asymmetric functionally and/or adopt different conformations of the two subunits in available X-ray structures.

DOI10.1021/ja206967d
Alternate JournalJ. Am. Chem. Soc.
PubMed ID22074452