1pgy
From Proteopedia
(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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'''Solution structure of the UBA domain in Saccharomyces cerevisiae protein, Swa2p'''<br /> | '''Solution structure of the UBA domain in Saccharomyces cerevisiae protein, Swa2p'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The SWA2/AUX1 gene has been proposed to encode the Saccharomyces | + | 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== | ==About this Structure== | ||
| - | 1PGY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http:// | + | 1PGY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PGY OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Chim, N.]] | [[Category: Chim, N.]] | ||
| - | [[Category: Gall, W | + | [[Category: Gall, W E.]] |
| - | [[Category: Graham, T | + | [[Category: Graham, T R.]] |
| - | [[Category: Harris, M | + | [[Category: Harris, M P.]] |
| - | [[Category: Krezel, A | + | [[Category: Krezel, A M.]] |
[[Category: Xiao, J.]] | [[Category: Xiao, J.]] | ||
[[Category: auxilin]] | [[Category: auxilin]] | ||
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[[Category: ubiquitin-associated domain]] | [[Category: ubiquitin-associated domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:28:45 2008'' |
Revision as of 12:28, 21 February 2008
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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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