2XEW

Crystal structure of K11-linked diubiquitin

Summary for 2XEW

• Entry DOI: 10.2210/pdb2xew/pdb
• Related: 1C3T 1D3Z 1F9J 1FXT 1G6J 1GJZ 1NBF 1OGW 1Q5W 1S1Q 1SIF 1TBE 1UBI 1UBQ 1XD3 1XQQ 1YX5 1YX6 1ZGU 2AYO 2BGF 2G45 2GBJ 2GBK 2GBM 2GBN 2J7Q 2JF5 2W9N 2WDT
• Descriptor: UBIQUITIN, 1,2-ETHANEDIOL, CHLORIDE ION, ... (5 entities in total)
• Functional Keywords: protein degradation, proteasome, cell cycle, deubiquitination
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 12
• Total formula weight: 104603.50

Authors

Bremm, A.,Freund, S.M.V.,Komander, D. (deposition date: 2010-05-18, release date: 2010-07-14, Last modification date: 2023-12-20)

Primary citation

Bremm, A.,Freund, S.M.V.,Komander, D.
Lys11-Linked Ubiquitin Chains Adopt Compact Conformations and are Preferentially Hydrolyzed by the Deubiquitinase Cezanne
Nat.Struct.Mol.Biol., 17:939-, 2010

PubMed Abstract: Ubiquitin is a versatile cellular signaling molecule that can form polymers of eight different linkages, and individual linkage types have been associated with distinct cellular functions. Though little is currently known about Lys11-linked ubiquitin chains, recent data indicate that they may be as abundant as Lys48 linkages and may be involved in vital cellular processes. Here we report the generation of Lys11-linked polyubiquitin in vitro, for which the Lys11-specific E2 enzyme UBE2S was fused to a ubiquitin binding domain. Crystallographic and NMR analyses of Lys11-linked diubiquitin reveal that Lys11-linked chains adopt compact conformations in which Ile44 is solvent exposed. Furthermore, we identify the OTU family deubiquitinase Cezanne as the first deubiquitinase with Lys11-linkage preference. Our data highlight the intrinsic specificity of the ubiquitin system that extends to Lys11-linked chains and emphasize that differentially linked polyubiquitin chains must be regarded as independent post-translational modifications.

PubMed: 20622874
DOI: 10.1038/NSMB.1873

Experimental method

X-RAY DIFFRACTION (2.2 Å)