5GOK

K11/K63-branched tri-Ubiquitin

Summary for 5GOK

• Entry DOI: 10.2210/pdb5gok/pdb
• Related: 5GO7 5GO8 5GOB 5GOC 5GOD 5GOG 5GOH 5GOI 5GOJ
• Descriptor: Ubiquitin, D-ubiquitin (3 entities in total)
• Functional Keywords: polyubiquitin chains, quasi-racemic crystal, protein binding
• Biological source: Homo sapiens (Human); More
• Cellular location: Ubiquitin: Cytoplasm : P0CG47
• Total number of polymer chains: 2
• Total formula weight: 17128.58

Authors

Gao, S.,Pan, M.,Zheng, Y.,Liu, L. (deposition date: 2016-07-27, release date: 2016-11-02, Last modification date: 2023-11-15)

Primary citation

Gao, S.,Pan, M.,Zheng, Y.,Huang, Y.,Zheng, Q.,Sun, D.,Lu, L.,Tan, X.,Tan, X.,Lan, H.,Wang, J.,Wang, T.,Wang, J.,Liu, L.
Monomer/Oligomer Quasi-Racemic Protein Crystallography
J.Am.Chem.Soc., 138:14497-14502, 2016

PubMed 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.

PubMed: 27768314
DOI: 10.1021/jacs.6b09545

Experimental method

X-RAY DIFFRACTION (1.84 Å)