Monomer/Oligomer Quasi-Racemic Protein Crystallography

Models, Molecular Ubiquitin Stereoisomerism Amino Acid Sequence Protein Multimerization Crystallography, X-Ray Protein Structure, Quaternary 01 natural sciences 0104 chemical sciences
DOI: 10.1021/jacs.6b09545 Publication Date: 2016-10-21T19:38:07Z
ABSTRACT
Racemic or quasi-racemic crystallography recently emerges as a useful technology for solution of the crystal structures of biomacromolecules. It remains unclear to what extent the biomacromolecules of opposite handedness can differ from each other in racemic or quasi-racemic crystallography. Here we report a finding that monomeric d-ubiquitin (Ub) has propensity to cocrystallize with different dimers, trimers, and even a tetramer of l-Ub. In these cocrystals the unconnected monomeric d-Ubs can self-assemble to form pseudomirror images of different oligomers of l-Ub. This monomer/oligomer cocrystallization phenomenon expands the concept of racemic crystallography. Using the monomer/oligomer cocrystallization technology we obtained, for the first time the X-ray structures of linear M1-linked tri- and tetra-Ubs and a K11/K63-branched tri-Ub.
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