|
|
| Line 3: |
Line 3: |
| | <StructureSection load='1vjv' size='340' side='right'caption='[[1vjv]], [[Resolution|resolution]] 1.74Å' scene=''> | | <StructureSection load='1vjv' size='340' side='right'caption='[[1vjv]], [[Resolution|resolution]] 1.74Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1vjv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VJV OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1VJV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1vjv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VJV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VJV FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">UBP6, YFR010W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=1vjv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vjv OCA], [https://pdbe.org/1vjv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vjv RCSB], [https://www.ebi.ac.uk/pdbsum/1vjv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vjv ProSAT], [https://www.topsan.org/Proteins/JCSG/1vjv TOPSAN]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitin_thiolesterase Ubiquitin thiolesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.15 3.1.2.15] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1vjv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vjv OCA], [http://pdbe.org/1vjv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1vjv RCSB], [http://www.ebi.ac.uk/pdbsum/1vjv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1vjv ProSAT], [http://www.topsan.org/Proteins/JCSG/1vjv TOPSAN]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/UBP6_YEAST UBP6_YEAST]] Predominant proteasome-associated deubiquitinase which releases ubiquitin from the proteasome targeted ubiquitinated proteins. Ensures the regeneration of ubiquitin at the proteasome. Has proteasome-inhibitory activity and delays the degradation of ubiquitinated proteins to provide a time window allowing gradual deubiquitination of the substrate. Stabilizes the association of HUL5 with proteasomes and works in opposition to polyubiquitin elongation activity of HUL5.<ref>PMID:9344467</ref> <ref>PMID:10527495</ref> <ref>PMID:12408819</ref> <ref>PMID:14581483</ref> <ref>PMID:17018280</ref> <ref>PMID:17190603</ref> | + | [https://www.uniprot.org/uniprot/UBP6_YEAST UBP6_YEAST] Predominant proteasome-associated deubiquitinase which releases ubiquitin from the proteasome targeted ubiquitinated proteins. Ensures the regeneration of ubiquitin at the proteasome. Has proteasome-inhibitory activity and delays the degradation of ubiquitinated proteins to provide a time window allowing gradual deubiquitination of the substrate. Stabilizes the association of HUL5 with proteasomes and works in opposition to polyubiquitin elongation activity of HUL5.<ref>PMID:9344467</ref> <ref>PMID:10527495</ref> <ref>PMID:12408819</ref> <ref>PMID:14581483</ref> <ref>PMID:17018280</ref> <ref>PMID:17190603</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 25: |
Line 23: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ubiquitin thiolesterase]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Structural genomic]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Jcsg]]
| + | |
| - | [[Category: PSI, Protein structure initiative]]
| + | |
| - | [[Category: Ubiquitin carboxyl-terminal hydrolase 6]]
| + | |
| - | [[Category: Yfr010w]]
| + | |
| Structural highlights
Function
UBP6_YEAST Predominant proteasome-associated deubiquitinase which releases ubiquitin from the proteasome targeted ubiquitinated proteins. Ensures the regeneration of ubiquitin at the proteasome. Has proteasome-inhibitory activity and delays the degradation of ubiquitinated proteins to provide a time window allowing gradual deubiquitination of the substrate. Stabilizes the association of HUL5 with proteasomes and works in opposition to polyubiquitin elongation activity of HUL5.[1] [2] [3] [4] [5] [6]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Park KC, Woo SK, Yoo YJ, Wyndham AM, Baker RT, Chung CH. Purification and characterization of UBP6, a new ubiquitin-specific protease in Saccharomyces cerevisiae. Arch Biochem Biophys. 1997 Nov 1;347(1):78-84. PMID:9344467 doi:http://dx.doi.org/10.1006/abbi.1997.0311
- ↑ Layfield R, Franklin K, Landon M, Walker G, Wang P, Ramage R, Brown A, Love S, Urquhart K, Muir T, Baker R, Mayer RJ. Chemically synthesized ubiquitin extension proteins detect distinct catalytic capacities of deubiquitinating enzymes. Anal Biochem. 1999 Oct 1;274(1):40-9. PMID:10527495 doi:http://dx.doi.org/10.1006/abio.1999.4234
- ↑ Leggett DS, Hanna J, Borodovsky A, Crosas B, Schmidt M, Baker RT, Walz T, Ploegh H, Finley D. Multiple associated proteins regulate proteasome structure and function. Mol Cell. 2002 Sep;10(3):495-507. PMID:12408819
- ↑ Guterman A, Glickman MH. Complementary roles for Rpn11 and Ubp6 in deubiquitination and proteolysis by the proteasome. J Biol Chem. 2004 Jan 16;279(3):1729-38. Epub 2003 Oct 27. PMID:14581483 doi:http://dx.doi.org/10.1074/jbc.M307050200
- ↑ Hanna J, Hathaway NA, Tone Y, Crosas B, Elsasser S, Kirkpatrick DS, Leggett DS, Gygi SP, King RW, Finley D. Deubiquitinating enzyme Ubp6 functions noncatalytically to delay proteasomal degradation. Cell. 2006 Oct 6;127(1):99-111. PMID:17018280 doi:http://dx.doi.org/10.1016/j.cell.2006.07.038
- ↑ Crosas B, Hanna J, Kirkpatrick DS, Zhang DP, Tone Y, Hathaway NA, Buecker C, Leggett DS, Schmidt M, King RW, Gygi SP, Finley D. Ubiquitin chains are remodeled at the proteasome by opposing ubiquitin ligase and deubiquitinating activities. Cell. 2006 Dec 29;127(7):1401-13. PMID:17190603 doi:http://dx.doi.org/10.1016/j.cell.2006.09.051
|
