5ln1

From Proteopedia

(Difference between revisions)

Revision as of 13:07, 10 May 2019

STRUCTURE OF UBIQUITYLATED-RPN10 FROM YEAST;

Structural highlights

5ln1 is a 2 chain structure with sequence from Baker's yeast and Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	RPN10, MCB1, SUN1, YHR200W (Baker's yeast), UBB (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[RPN10_YEAST] Multiubiquitin binding protein. [UBB_HUMAN] Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.^[1] ^[2]

Publication Abstract from PubMed

Ubiquitin receptors decode ubiquitin signals into many cellular responses. Ubiquitin receptors also undergo coupled monoubiquitylation, and rapid deubiquitylation has hampered the characterization of the ubiquitylated state. Using bacteria that express a ubiquitylation apparatus, we purified and determined the crystal structure of the proteasomal ubiquitin-receptor Rpn10 in its ubiquitylated state. The structure shows a novel ubiquitin-binding patch that directs K84 ubiquitylation. Superimposition of ubiquitylated-Rpn10 onto electron-microscopy models of proteasomes indicates that the Rpn10-conjugated ubiquitin clashes with Rpn9, suggesting that ubiquitylation might be involved in releasing Rpn10 from the proteasome. Indeed, ubiquitylation on immobilized proteasomes dissociates the modified Rpn10 from the complex, while unmodified Rpn10 mainly remains associated. In vivo experiments indicate that contrary to wild type, Rpn10-K84R is stably associated with the proteasomal subunit Rpn9. Similarly Rpn10, but not ubiquitylated-Rpn10, binds Rpn9 in vitro. Thus we suggest that ubiquitylation functions to dissociate modified ubiquitin receptors from their targets, a function that promotes cyclic activity of ubiquitin receptors.

Structure of ubiquitylated-Rpn10 provides insight into its autoregulation mechanism.,Keren-Kaplan T, Zeev Peters L, Levin-Kravets O, Attali I, Kleifeld O, Shohat N, Artzi S, Zucker O, Pilzer I, Reis N, Glickman MH, Ben-Aroya S, Prag G Nat Commun. 2016 Oct 4;7:12960. doi: 10.1038/ncomms12960. PMID:27698474^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Huang F, Kirkpatrick D, Jiang X, Gygi S, Sorkin A. Differential regulation of EGF receptor internalization and degradation by multiubiquitination within the kinase domain. Mol Cell. 2006 Mar 17;21(6):737-48. PMID:16543144 doi:S1097-2765(06)00120-1
↑ Komander D. The emerging complexity of protein ubiquitination. Biochem Soc Trans. 2009 Oct;37(Pt 5):937-53. doi: 10.1042/BST0370937. PMID:19754430 doi:10.1042/BST0370937
↑ Keren-Kaplan T, Zeev Peters L, Levin-Kravets O, Attali I, Kleifeld O, Shohat N, Artzi S, Zucker O, Pilzer I, Reis N, Glickman MH, Ben-Aroya S, Prag G. Structure of ubiquitylated-Rpn10 provides insight into its autoregulation mechanism. Nat Commun. 2016 Oct 4;7:12960. doi: 10.1038/ncomms12960. PMID:27698474 doi:http://dx.doi.org/10.1038/ncomms12960

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5ln1"

@@ Line 1: / Line 1: @@
 ==STRUCTURE OF UBIQUITYLATED-RPN10 FROM YEAST;==
-<StructureSection load='5ln1' size='340' side='right' caption='[[5ln1]], [[Resolution|resolution]] 3.14&Aring;' scene=''>
+<StructureSection load='5ln1' size='340' side='right'caption='[[5ln1]], [[Resolution|resolution]] 3.14&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5ln1]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LN1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LN1 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5ln1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LN1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LN1 FirstGlance]. <br>
-</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=5ln1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ln1 OCA], [http://pdbe.org/5ln1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ln1 RCSB], [http://www.ebi.ac.uk/pdbsum/5ln1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ln1 ProSAT]</span></td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RPN10, MCB1, SUN1, YHR200W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), UBB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5ln1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ln1 OCA], [http://pdbe.org/5ln1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ln1 RCSB], [http://www.ebi.ac.uk/pdbsum/5ln1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ln1 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
 </div>
 <div class="pdbe-citations 5ln1" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Proteasome|Proteasome]]
+*[[Ubiquitin|Ubiquitin]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Baker's yeast]]
+[[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Attali, I]]
 [[Category: Keren-Kaplan, T]]

5ln1

From Proteopedia

Revision as of 13:07, 10 May 2019

STRUCTURE OF UBIQUITYLATED-RPN10 FROM YEAST;

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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