1pgy

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|ACTIVITY=
|ACTIVITY=
|GENE= SWA2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
|GENE= SWA2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pgy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pgy OCA], [http://www.ebi.ac.uk/pdbsum/1pgy PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pgy RCSB]</span>
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[[Category: ubiquitin-associated domain]]
[[Category: ubiquitin-associated domain]]
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Revision as of 19:59, 30 March 2008


PDB ID 1pgy

Drag the structure with the mouse to rotate
Gene: SWA2 (Saccharomyces cerevisiae)
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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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