2D3G

Double sided ubiquitin binding of Hrs-UIM

Summary for 2D3G

• Entry DOI: 10.2210/pdb2d3g/pdb
• Descriptor: ubiquitin, ubiquitin interacting motif from hepatocyte growth factor-regulated tyrosine kinase substrate (3 entities in total)
• Functional Keywords: protein-protein complex, uim and ubiquitin, protein transport
• Biological source: Bos taurus (cattle); More
• Cellular location: Cytoplasm: O14964
• Total number of polymer chains: 3
• Total formula weight: 19542.22

Authors

Hirano, S.,Kawasaki, M.,Kato, R.,Wakatsuki, S. (deposition date: 2005-09-28, release date: 2005-12-20, Last modification date: 2023-10-25)

Primary citation

Hirano, S.,Kawasaki, M.,Ura, H.,Kato, R.,Raiborg, C.,Stenmark, H.,Wakatsuki, S.
Double-sided ubiquitin binding of Hrs-UIM in endosomal protein sorting
Nat.Struct.Mol.Biol., 13:272-277, 2006

PubMed Abstract: Hrs has an essential role in sorting of monoubiquitinated receptors to multivesicular bodies for lysosomal degradation, through recognition of ubiquitinated receptors by its ubiquitin-interacting motif (UIM). Here, we present the structure of a complex of Hrs-UIM and ubiquitin at 1.7-A resolution. Hrs-UIM forms a single alpha-helix, which binds two ubiquitin molecules, one on either side. These two ubiquitin molecules are related by pseudo two-fold screw symmetry along the helical axis of the UIM, corresponding to a shift by two residues on the UIM helix. Both ubiquitin molecules interact with the UIM in the same manner, using the Ile44 surface, with equal binding affinities. Mutational experiments show that both binding sites of Hrs-UIM are required for efficient degradative protein sorting. Hrs-UIM belongs to a new subclass of double-sided UIMs, in contrast to its yeast homolog Vps27p, which has two tandem single-sided UIMs.

PubMed: 16462748
DOI: 10.1038/nsmb1051

Experimental method

X-RAY DIFFRACTION (1.7 Å)