1P0R

Solution Structure of UBL5 a human Ubiquitin-Like Protein

Summary for 1P0R

• Entry DOI: 10.2210/pdb1p0r/pdb
• Descriptor: ubiquitin-like 5 (1 entity in total)
• Functional Keywords: ubiquitin-like fold, protein binding
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: Q9BZL1
• Total number of polymer chains: 1
• Total formula weight: 10732.31

Authors

McNally, T.,Huang, Q.,Janis, R.S.,Liu, Z.,Olejniczak, E.T.,Reilly, R.M. (deposition date: 2003-04-10, release date: 2003-10-28, Last modification date: 2024-05-22)

Primary citation

McNally, T.,Huang, Q.,Janis, R.S.,Liu, Z.,Olejniczak, E.T.,Reilly, R.M.
Structural analysis of UBL5, a novel ubiquitin-like modifier
Protein Sci., 12:1562-1566, 2003

PubMed Abstract: UBL5 is a widely expressed human protein that is strongly conserved across phylogeny. Orthologs of UBL5 occur in every eukaryotic genome characterized to date. The yeast ortholog of UBL5, HUB1, was reported to be a ubiquitin-like protein modifier important for modulation of protein function. However, unlike ubiquitin and all other ubiquitin-like modifiers, UBL5 and its yeast ortholog HUB1 both contain a C-terminal di-tyrosine motif followed by a single variable residue instead of the characteristic di-glycine found in all other ubiquitin-like modifiers. Here we describe the three-dimensional structure of UBL5 determined by NMR. The overall structure of the protein was found to be very similar to ubiquitin despite the low approximately 25% residue similarity. The signature C-terminal di-tyrosine residues in UBL5 are involved in the final beta sheet of the protein. This is very different to the di-glycine motif found in ubiquitin, which extends beyond the final beta sheet. In addition, we have confirmed an earlier report of an interaction between UBL5 and the cyclin-like kinase, CLK4, which we have determined is specific and does not extend to other cyclin-like kinase family members.

PubMed: 12824502
DOI: 10.1110/ps.0382803

Experimental method

SOLUTION NMR