1pgy
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(New page: 200px<br /><applet load="1pgy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pgy" /> '''Solution structure of the UBA domain in Sacc...)
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Revision as of 21:40, 20 November 2007
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Solution structure of the UBA domain in Saccharomyces cerevisiae protein, Swa2p
Overview
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.
About this Structure
1PGY is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Solution structure of the ubiquitin-binding domain in Swa2p from Saccharomyces cerevisiae., Chim N, Gall WE, Xiao J, Harris MP, Graham TR, Krezel AM, Proteins. 2004 Mar 1;54(4):784-93. PMID:14997574
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