5VMD

Crystal structure of UBR-box from UBR6 in a domain-swapping conformation

Summary for 5VMD

• Entry DOI: 10.2210/pdb5vmd/pdb
• Descriptor: F-box only protein 11, ZINC ION, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: domain swapping, zinc finger, zinc, ubr-box, ubr6, fbxo11, ligase
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 4
• Total formula weight: 35961.32

Authors

Munoz-Escobar, J.,Kozlov, G.,Gehring, K. (deposition date: 2017-04-27, release date: 2017-07-12, Last modification date: 2024-03-13)

Primary citation

Munoz-Escobar, J.,Kozlov, G.,Gehring, K.
Crystal structure of the UBR-box from UBR6/FBXO11 reveals domain swapping mediated by zinc binding.
Protein Sci., 26:2092-2097, 2017

PubMed Abstract: The UBR-box is a 70-residue zinc finger domain present in the UBR family of E3 ubiquitin ligases that directly binds N-terminal degradation signals in substrate proteins. UBR6, also called FBXO11, is an UBR-box containing E3 ubiquitin ligase that does not bind N-terminal signals. Here, we present the crystal structure of the UBR-box domain from human UBR6. The dimeric crystal structure reveals a unique form of domain swapping mediated by zinc coordination, where three independent protein chains come together to regenerate the topology of the monomeric UBR-box fold. Analysis of the structure suggests that the absence of N-terminal residue binding arises from the lack of an amino acid binding pocket.

PubMed: 28691247
DOI: 10.1002/pro.3227

Experimental method

X-RAY DIFFRACTION (2.202 Å)