title: Solution NMR evidence for symmetry in functionally or crystallographically asymmetric homodimers.
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.
authors.affiliation: Department of Chemistry and Biochemistry, University of Maryland, College Park, Maryland 20742, USA.
authors.forename: Raquel
authors.initials: R
authors.lastname: Godoy-Ruiz
authors.forename: Anna
authors.initials: A
authors.lastname: Krejcirikova
authors.forename: D Travis
authors.initials: DT
authors.lastname: Gallagher
authors.forename: Vitali
authors.initials: V
authors.lastname: Tugarinov
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D018360:Crystallography, X-Ray; D002373:Cyclic AMP Receptor Protein / Q000737:chemistry; D001411:Geobacillus stearothermophilus / Q000737:chemistry*; D008958:Models, Molecular; D009169:Mycobacterium tuberculosis / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011487:Protein Conformation; D055503:Protein Multimerization
chemical_list: D001426:Bacterial Proteins; C513697:CRP protein, Mycobacterium tuberculosis; D002373:Cyclic AMP Receptor Protein