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| | ==Solution Structure of the N-terminal Domain of the Yeast Rpn5== | | ==Solution Structure of the N-terminal Domain of the Yeast Rpn5== |
| - | <StructureSection load='5zmr' size='340' side='right'caption='[[5zmr]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='5zmr' size='340' side='right'caption='[[5zmr]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5zmr]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZMR OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5ZMR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5zmr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZMR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZMR FirstGlance]. <br> |
| - | </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=5zmr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zmr OCA], [http://pdbe.org/5zmr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zmr RCSB], [http://www.ebi.ac.uk/pdbsum/5zmr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zmr ProSAT]</span></td></tr> | + | </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=5zmr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zmr OCA], [https://pdbe.org/5zmr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zmr RCSB], [https://www.ebi.ac.uk/pdbsum/5zmr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zmr ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RPN5_YEAST RPN5_YEAST]] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.<ref>PMID:9426256</ref> | + | [https://www.uniprot.org/uniprot/RPN5_YEAST RPN5_YEAST] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.<ref>PMID:9426256</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hu, Y]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Jin, C]] | + | [[Category: Hu Y]] |
| - | [[Category: Li, H]] | + | [[Category: Jin C]] |
| - | [[Category: Zhang, W]] | + | [[Category: Li H]] |
| - | [[Category: Zhao, C]] | + | [[Category: Zhang W]] |
| - | [[Category: A-helix bundle]]
| + | [[Category: Zhao C]] |
| - | [[Category: Hydrolase]]
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| Structural highlights
Function
RPN5_YEAST Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.[1]
Publication Abstract from PubMed
The 26S proteasome is the major protein degradation machinery in living cells. The Rpn5 protein is one scaffolding subunit in the lid subcomplex of the 19S regulatory particle in the proteasome holoenzyme. Herein we report the solution structure of the N-terminal domain (NTD) of yeast Rpn5 at high resolution by NMR spectroscopy. The results show that Rpn5 NTD adopts alpha-solenoid-like fold in right-handed superhelical configuration formed by a number of alpha-helices. Structural comparisons with currently available cryo-EM structures reveal local structural differences in the first three helices between yeast and human Rpn5. The results further highlight the conformational flexibility in three possible protein interaction sites. Moreover, the structures of the NTD show large variations among different PCI-containing Rpn subunits. Our current results provide atomic-level structural basis for further investigations of protein-protein interactions and the proteasome assembly pathway.
Solution structure of the N-terminal domain of proteasome lid subunit Rpn5.,Zhang W, Zhao C, Hu Y, Jin C Biochem Biophys Res Commun. 2018 Sep 26;504(1):225-230. doi:, 10.1016/j.bbrc.2018.08.159. Epub 2018 Sep 1. PMID:30177392[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Saito A, Watanabe TK, Shimada Y, Fujiwara T, Slaughter CA, DeMartino GN, Tanahashi N, Tanaka K. cDNA cloning and functional analysis of p44.5 and p55, two regulatory subunits of the 26S proteasome. Gene. 1997 Dec 12;203(2):241-50. PMID:9426256
- ↑ Zhang W, Zhao C, Hu Y, Jin C. Solution structure of the N-terminal domain of proteasome lid subunit Rpn5. Biochem Biophys Res Commun. 2018 Sep 26;504(1):225-230. doi:, 10.1016/j.bbrc.2018.08.159. Epub 2018 Sep 1. PMID:30177392 doi:http://dx.doi.org/10.1016/j.bbrc.2018.08.159
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