5GOI: Lys48-linked Di-ubiquitin

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.
PDB ID: 5GOIDownload
MMDB ID: 144523
PDB Deposition Date: 2016/7/27
Updated in MMDB: 2016/11
Experimental Method:
x-ray diffraction
Resolution: 1.59  Å
Source Organism:
Similar Structures:
Biological Unit for 5GOI: tetrameric; determined by author
Molecular Components in 5GOI
Label Count Molecule
Proteins (2 molecules)
Ubiquitin(Gene symbol: UBB)
Molecule annotation
Nucleotide(1 molecule)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB