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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'''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==
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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.
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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==
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PGY OCA].
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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.]]
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[[Category: Gall, W.E.]]
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[[Category: Gall, W E.]]
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[[Category: Graham, T.R.]]
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[[Category: Graham, T R.]]
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[[Category: Harris, M.P.]]
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[[Category: Harris, M P.]]
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[[Category: Krezel, A.M.]]
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[[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]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:47:58 2007''
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''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


1pgy

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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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