5zmr

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'''Unreleased structure'''
 
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The entry 5zmr is ON HOLD until Paper Publication
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==Solution Structure of the N-terminal Domain of the Yeast Rpn5==
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<StructureSection load='5zmr' size='340' side='right' caption='[[5zmr]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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== Structural highlights ==
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<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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZMR FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/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>
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</table>
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== Function ==
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[[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors:
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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<ref>PMID:30177392</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5zmr" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Hu, Y]]
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[[Category: Jin, C]]
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[[Category: Li, H]]
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[[Category: Zhang, W]]
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[[Category: Zhao, C]]
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[[Category: A-helix bundle]]
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[[Category: Hydrolase]]

Revision as of 07:58, 26 September 2018

Solution Structure of the N-terminal Domain of the Yeast Rpn5

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