|
|
| Line 1: |
Line 1: |
| | | | |
| | ==Solution structure of the UBA domain in Saccharomyces cerevisiae protein, Swa2p== | | ==Solution structure of the UBA domain in Saccharomyces cerevisiae protein, Swa2p== |
| - | <StructureSection load='1pgy' size='340' side='right'caption='[[1pgy]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='1pgy' size='340' side='right'caption='[[1pgy]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1pgy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PGY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PGY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1pgy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PGY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PGY FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SWA2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1pgy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pgy OCA], [https://pdbe.org/1pgy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pgy RCSB], [https://www.ebi.ac.uk/pdbsum/1pgy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pgy ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1pgy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pgy OCA], [https://pdbe.org/1pgy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pgy RCSB], [https://www.ebi.ac.uk/pdbsum/1pgy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pgy ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/SWA2_YEAST SWA2_YEAST]] Cofactor for the uncoating of clathrin-coated vesicles (CCVs) by Hsp70-type chaperones (SSA1/2/3 and SSB1/2). Coat disassembly is important for fusion of vesicles with target membranes and for recycling components of clathrin coats to the cytoplasm for further rounds of vesicle formation. Binds to assembled clathrin and recruits the ATP-activated chaperone to CCVs. Stimulates the ATPase activity of the clathrin-associated Hsp70-type chaperone SSA1, which then disrupts clathrin-clathrin interactions, leading to release of the clathrin coat. In addition, prevents unproductive clathrin assembly in the cell. Also required for cortical endoplasmic reticulum inheritance.<ref>PMID:11084334</ref> <ref>PMID:11146663</ref> <ref>PMID:11553703</ref>
| + | [https://www.uniprot.org/uniprot/SWA2_YEAST SWA2_YEAST] Cofactor for the uncoating of clathrin-coated vesicles (CCVs) by Hsp70-type chaperones (SSA1/2/3 and SSB1/2). Coat disassembly is important for fusion of vesicles with target membranes and for recycling components of clathrin coats to the cytoplasm for further rounds of vesicle formation. Binds to assembled clathrin and recruits the ATP-activated chaperone to CCVs. Stimulates the ATPase activity of the clathrin-associated Hsp70-type chaperone SSA1, which then disrupts clathrin-clathrin interactions, leading to release of the clathrin coat. In addition, prevents unproductive clathrin assembly in the cell. Also required for cortical endoplasmic reticulum inheritance.<ref>PMID:11084334</ref> <ref>PMID:11146663</ref> <ref>PMID:11553703</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 22: |
Line 22: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chim, N]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Gall, W E]] | + | [[Category: Chim N]] |
| - | [[Category: Graham, T R]] | + | [[Category: Gall WE]] |
| - | [[Category: Harris, M P]] | + | [[Category: Graham TR]] |
| - | [[Category: Krezel, A M]] | + | [[Category: Harris MP]] |
| - | [[Category: Xiao, J]] | + | [[Category: Krezel AM]] |
| - | [[Category: Auxilin]]
| + | [[Category: Xiao J]] |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: Swa2]]
| + | |
| - | [[Category: Uba]]
| + | |
| - | [[Category: Ubiquitin]]
| + | |
| - | [[Category: Ubiquitin-associated domain]]
| + | |
| Structural highlights
Function
SWA2_YEAST Cofactor for the uncoating of clathrin-coated vesicles (CCVs) by Hsp70-type chaperones (SSA1/2/3 and SSB1/2). Coat disassembly is important for fusion of vesicles with target membranes and for recycling components of clathrin coats to the cytoplasm for further rounds of vesicle formation. Binds to assembled clathrin and recruits the ATP-activated chaperone to CCVs. Stimulates the ATPase activity of the clathrin-associated Hsp70-type chaperone SSA1, which then disrupts clathrin-clathrin interactions, leading to release of the clathrin coat. In addition, prevents unproductive clathrin assembly in the cell. Also required for cortical endoplasmic reticulum inheritance.[1] [2] [3]
Publication Abstract from PubMed
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.
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[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Gall WE, Higginbotham MA, Chen C, Ingram MF, Cyr DM, Graham TR. The auxilin-like phosphoprotein Swa2p is required for clathrin function in yeast. Curr Biol. 2000 Nov 2;10(21):1349-58. PMID:11084334
- ↑ Pishvaee B, Costaguta G, Yeung BG, Ryazantsev S, Greener T, Greene LE, Eisenberg E, McCaffery JM, Payne GS. A yeast DNA J protein required for uncoating of clathrin-coated vesicles in vivo. Nat Cell Biol. 2000 Dec;2(12):958-63. PMID:11146663 doi:http://dx.doi.org/10.1038/35046619
- ↑ Du Y, Pypaert M, Novick P, Ferro-Novick S. Aux1p/Swa2p is required for cortical endoplasmic reticulum inheritance in Saccharomyces cerevisiae. Mol Biol Cell. 2001 Sep;12(9):2614-28. PMID:11553703
- ↑ Chim N, Gall WE, Xiao J, Harris MP, Graham TR, Krezel AM. Solution structure of the ubiquitin-binding domain in Swa2p from Saccharomyces cerevisiae. Proteins. 2004 Mar 1;54(4):784-93. PMID:14997574 doi:http://dx.doi.org/10.1002/prot.10636
|
