4S1Z: Crystal Structure Of Trabid Nzf1 In Complex With K29 Linked Di- Ubiquitin

Citation:
Abstract
Polyubiquitin chains regulate diverse cellular processes through the ability of ubiquitin to form chains of eight different linkage types. Although detected in yeast and mammals, little is known about K29-linked polyubiquitin. Here we report the generation of K29 chains in vitro using a ubiquitin chain-editing complex consisting of the HECT E3 ligase UBE3C and the deubiquitinase vOTU. We determined the crystal structure of K29-linked diubiquitin, which adopts an extended conformation with the hydrophobic patches on both ubiquitin moieties exposed and available for binding. Indeed, the crystal structure of the NZF1 domain of TRABID in complex with K29 chains reveals a binding mode that involves the hydrophobic patch on only one of the ubiquitin moieties and exploits the flexibility of K29 chains to achieve linkage selective binding. Further, we establish methods to study K29-linked polyubiquitin and find that K29 linkages exist in cells within mixed or branched chains containing other linkages.
PDB ID: 4S1ZDownload
MMDB ID: 128410
PDB Deposition Date: 2015/1/16
Updated in MMDB: 2015/04
Experimental Method:
x-ray diffraction
Resolution: 3.03  Å
Source Organism:
Bos taurus
Similar Structures:
Biological Unit for 4S1Z: dimeric; determined by author
Molecular Components in 4S1Z
Label Count Molecule
Proteins (2 molecules)
1
Ubiquitin(Gene symbol: UBA52)
Molecule annotation
1
Ubiquitin Thioesterase Zranb1(Gene symbol: ZRANB1)
Molecule annotation
Chemical (1 molecule)
1
1
* Click molecule labels to explore molecular sequence information.

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