5irs

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'''Unreleased structure'''
 
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The entry 5irs is ON HOLD until Paper Publication
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==crystal structure of the proteasomal Rpn13 PRU-domain==
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<StructureSection load='5irs' size='340' side='right' caption='[[5irs]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5irs]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IRS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5IRS FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene></td></tr>
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<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=5irs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5irs OCA], [http://pdbe.org/5irs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5irs RCSB], [http://www.ebi.ac.uk/pdbsum/5irs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5irs ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/ADRM1_HUMAN ADRM1_HUMAN]] Functions as a proteasomal ubiquitin receptor. Recruits the deubiquitinating enzyme UCHL5 at the 26S proteasome and promotes its activity.<ref>PMID:16990800</ref> <ref>PMID:17139257</ref> <ref>PMID:16815440</ref> <ref>PMID:16906146</ref> <ref>PMID:18497817</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Three receptors (Rpn1/S2/PSMD2, Rpn10/S5a, Rpn13/Adrm1) in the proteasome bind substrates by interacting with conjugated ubiquitin chains and/or shuttle factors (Rad23/HR23, Dsk2/PLIC/ubiquilin, Ddi1) that carry ubiquitinated substrates to proteasomes. We solved the structure of two such receptors with their preferred shuttle factor, namely hRpn13Pru:hPLIC2UBL and scRpn1 T1:scRad23UBL. We find that ubiquitin folds in Rad23 and Dsk2 are fine-tuned by residue substitutions to achieve high affinity for Rpn1 and Rpn13, respectively. A single substitution in hPLIC2 yields enhanced interactions with the Rpn13 ubiquitin contact surface and sterically blocks hRpn13 binding to its preferred ubiquitin chain type, K48-linked chains. Rpn1 T1 binds two ubiquitins in tandem and we find that Rad23 binds exclusively to the higher-affinity Helix28/Helix30 site. Rad23 contacts at Helix28/Helix30 are optimized compared to ubiquitin by multiple conservative amino acid substitutions. Thus, shuttle factors deliver substrates to proteasomes through fine-tuned ubiquitin-like surfaces.
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Authors:
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Structures of Rpn1 T1:Rad23 and hRpn13:hPLIC2 Reveal Distinct Binding Mechanisms between Substrate Receptors and Shuttle Factors of the Proteasome.,Chen X, Randles L, Shi K, Tarasov SG, Aihara H, Walters KJ Structure. 2016 Jul 6. pii: S0969-2126(16)30125-3. doi:, 10.1016/j.str.2016.05.018. PMID:27396824<ref>PMID:27396824</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 5irs" 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: Aihara, H]]
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[[Category: Chen, X]]
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[[Category: Shi, K]]
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[[Category: Walters, K]]
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[[Category: Protein binding]]
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[[Category: Ubiquitin]]

Revision as of 15:17, 26 July 2016

crystal structure of the proteasomal Rpn13 PRU-domain

5irs, resolution 1.80Å

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