6ISU

Crystal structure of Lys27-linked di-ubiquitin in complex with its selective interacting protein UCHL3

Summary for 6ISU

• Entry DOI: 10.2210/pdb6isu/pdb
• Descriptor: Ubiquitin carboxyl-terminal hydrolase isozyme L3, Ubiquitin, ... (4 entities in total)
• Functional Keywords: ubiquitination, uchl3, lys27-linked di-ubiquitin, hydrolase
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 3
• Total formula weight: 43384.27

Authors

Ding, S.,Pan, M.,Zheng, Q.,Ren, Y.,Hong, D. (deposition date: 2018-11-19, release date: 2019-02-06, Last modification date: 2023-11-22)

Primary citation

Pan, M.,Zheng, Q.,Ding, S.,Zhang, L.,Qu, Q.,Wang, T.,Hong, D.,Ren, Y.,Liang, L.,Chen, C.,Mei, Z.,Liu, L.
Chemical Protein Synthesis Enabled Mechanistic Studies on the Molecular Recognition of K27-linked Ubiquitin Chains.
Angew. Chem. Int. Ed. Engl., 58:2627-2631, 2019

PubMed Abstract: New synthetic strategies that exploited the strengths of both chemoselective ligation and recombinant protein expression were developed to prepare K27 di-ubiquitins (diUb), which enabled mechanistic studies on the molecular recognition of K27-linked Ubs by single-molecule Förster resonance energy transfer (smFRET) and X-ray crystallography. The results revealed that free K27 diUb adopted a compact conformation, whereas upon binding to UCHL3, K27 diUb was remodeled to an open conformation. The K27 isopeptide bond remained rigidly buried inside the diUb moiety during binding, an interesting unique structural feature that may explain the distinctive biological function of K27 Ub chains.

PubMed: 30589182
DOI: 10.1002/anie.201810814

Experimental method

X-RAY DIFFRACTION (1.866 Å)