1PGY

Solution structure of the UBA domain in Saccharomyces cerevisiae protein, Swa2p

Summary for 1PGY

• Entry DOI: 10.2210/pdb1pgy/pdb
• Descriptor: Swa2p (1 entity in total)
• Functional Keywords: uba, ubiquitin, swa2, auxilin, ubiquitin-associated domain, protein binding
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Cytoplasm: Q06677
• Total number of polymer chains: 1
• Total formula weight: 5547.27

Authors

Chim, N.,Gall, W.E.,Xiao, J.,Harris, M.P.,Graham, T.R.,Krezel, A.M. (deposition date: 2003-05-28, release date: 2004-03-23, Last modification date: 2024-05-22)

Primary citation

Chim, N.,Gall, W.E.,Xiao, J.,Harris, M.P.,Graham, T.R.,Krezel, A.M.
Solution structure of the ubiquitin-binding domain in Swa2p from Saccharomyces cerevisiae.
PROTEINS: STRUCT.,FUNCT.,GENET., 54:784-793, 2004

PubMed Abstract: The SWA2/AUX1 gene has been proposed to encode the Saccharomyces cerevisiae ortholog of mammalian auxilin. Swa2p is required for clathrin assembly/dissassembly in vivo, thereby implicating it in intracellular protein and lipid trafficking. While investigating the 287-residue N-terminal region of Swa2p, we found a single stably folded domain between residues 140 and 180. Using binding assays and structural analysis, we established this to be a ubiquitin-associated (UBA) domain, unidentified by bioinformatics of the yeast genome. We determined the solution structure of this Swa2p domain and found a characteristic three-helix UBA fold. Comparisons of structures of known UBA folds reveal that the position of the third helix is quite variable. This helix in Swa2p UBA contains a bulkier tyrosine in place of smaller residues found in other UBAs and cannot pack as close to the second helix. The molecular surface of Swa2p UBA has a mostly negative potential, with a single hydrophobic surface patch found also in the UBA domains of human protein, HHR23A. The presence of a UBA domain implicates Swa2p in novel roles involving ubiquitin and ubiquitinated substrates. We propose that Swa2p is a multifunctional protein capable of recognizing several proteins through its protein-protein recognition domains.

PubMed: 14997574
DOI: 10.1002/prot.10636

Experimental method

SOLUTION NMR