4jqu

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
'''Unreleased structure'''
+
{{STRUCTURE_4jqu| PDB=4jqu | SCENE= }}
 +
===Crystal structure of Ubc7p in complex with the U7BR of Cue1p===
 +
{{ABSTRACT_PUBMED_23665230}}
-
The entry 4jqu is ON HOLD until Paper Publication
+
==Function==
 +
[[http://www.uniprot.org/uniprot/UBC7_YEAST UBC7_YEAST]] Catalyzes the covalent attachment of ubiquitin to other proteins. Functions in degradation of misfolded or regulated proteins localized in the endoplasmic reticulum (ER) lumen or membrane via the ubiquitin-proteasome system. Cognate E2 conjugating enzyme for the DOA10 ubiquitin ligase complex, which is part of the ERAD-C pathway responsible for the rapid degradation of membrane proteins with misfolded cytoplasmic domains, and of the HRD1 ubiquitin ligase complex, which is part of the ERAD-L and ERAD-M pathways responsible for the rapid degradation of soluble lumenal and membrane proteins with misfolded lumenal domains (ERAD-L), or ER-membrane proteins with misfolded transmembrane domains (ERAD-M). Involved in resistance to cadmium poisoning.<ref>PMID:8393731</ref> <ref>PMID:9388185</ref> <ref>PMID:9695950</ref> <ref>PMID:11641273</ref> <ref>PMID:11390656</ref> <ref>PMID:11146622</ref> <ref>PMID:16873066</ref>
-
Authors: Liang, Y.-H., Metzger, M.B., Weissman, A.M., Ji, X.
+
==About this Structure==
 +
[[4jqu]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JQU OCA].
-
Description: Crystal structure of Ubc7p in complex with the U7BR of Cue1p
+
==Reference==
 +
<ref group="xtra">PMID:023665230</ref><references group="xtra"/><references/>
 +
[[Category: Saccharomyces cerevisiae s288c]]
 +
[[Category: Ubiquitin--protein ligase]]
 +
[[Category: Ji, X.]]
 +
[[Category: Liang, Y H.]]
 +
[[Category: Metzger, M B.]]
 +
[[Category: Weissman, A M.]]
 +
[[Category: Ligase-activator complex]]
 +
[[Category: Ligase-protein binding complex]]
 +
[[Category: Ubc7p:u7br complex]]

Revision as of 09:08, 19 June 2013

Template:STRUCTURE 4jqu

Contents

Crystal structure of Ubc7p in complex with the U7BR of Cue1p

Template:ABSTRACT PUBMED 23665230

Function

[UBC7_YEAST] Catalyzes the covalent attachment of ubiquitin to other proteins. Functions in degradation of misfolded or regulated proteins localized in the endoplasmic reticulum (ER) lumen or membrane via the ubiquitin-proteasome system. Cognate E2 conjugating enzyme for the DOA10 ubiquitin ligase complex, which is part of the ERAD-C pathway responsible for the rapid degradation of membrane proteins with misfolded cytoplasmic domains, and of the HRD1 ubiquitin ligase complex, which is part of the ERAD-L and ERAD-M pathways responsible for the rapid degradation of soluble lumenal and membrane proteins with misfolded lumenal domains (ERAD-L), or ER-membrane proteins with misfolded transmembrane domains (ERAD-M). Involved in resistance to cadmium poisoning.[1] [2] [3] [4] [5] [6] [7]

About this Structure

4jqu is a 2 chain structure with sequence from Saccharomyces cerevisiae s288c. Full crystallographic information is available from OCA.

Reference

  • Metzger MB, Liang YH, Das R, Mariano J, Li S, Li J, Kostova Z, Byrd RA, Ji X, Weissman AM. A Structurally Unique E2-Binding Domain Activates Ubiquitination by the ERAD E2, Ubc7p, through Multiple Mechanisms. Mol Cell. 2013 May 23;50(4):516-27. doi: 10.1016/j.molcel.2013.04.004. Epub 2013 , May 9. PMID:23665230 doi:10.1016/j.molcel.2013.04.004
  1. Chen P, Johnson P, Sommer T, Jentsch S, Hochstrasser M. Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MAT alpha 2 repressor. Cell. 1993 Jul 30;74(2):357-69. PMID:8393731
  2. Biederer T, Volkwein C, Sommer T. Role of Cue1p in ubiquitination and degradation at the ER surface. Science. 1997 Dec 5;278(5344):1806-9. PMID:9388185
  3. Johnson PR, Swanson R, Rakhilina L, Hochstrasser M. Degradation signal masking by heterodimerization of MATalpha2 and MATa1 blocks their mutual destruction by the ubiquitin-proteasome pathway. Cell. 1998 Jul 24;94(2):217-27. PMID:9695950
  4. Swanson R, Locher M, Hochstrasser M. A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matalpha2 repressor degradation. Genes Dev. 2001 Oct 15;15(20):2660-74. PMID:11641273 doi:10.1101/gad.933301
  5. Gardner RG, Shearer AG, Hampton RY. In vivo action of the HRD ubiquitin ligase complex: mechanisms of endoplasmic reticulum quality control and sterol regulation. Mol Cell Biol. 2001 Jul;21(13):4276-91. PMID:11390656 doi:10.1128/MCB.21.13.4276-4291.2001
  6. Bays NW, Gardner RG, Seelig LP, Joazeiro CA, Hampton RY. Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-associated degradation. Nat Cell Biol. 2001 Jan;3(1):24-9. PMID:11146622 doi:10.1038/35050524
  7. Carvalho P, Goder V, Rapoport TA. Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins. Cell. 2006 Jul 28;126(2):361-73. PMID:16873066 doi:10.1016/j.cell.2006.05.043

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools