This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2r2y

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2r2y.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2r2y.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2r2y| PDB=2r2y | SCENE= }}
{{STRUCTURE_2r2y| PDB=2r2y | SCENE= }}
-
'''Crystal structure of the proteasomal Rpn13 PRU-domain'''
+
===Crystal structure of the proteasomal Rpn13 PRU-domain===
-
==Overview==
+
<!--
-
Targeted protein degradation is largely performed by the ubiquitin-proteasome pathway, in which substrate proteins are marked by covalently attached ubiquitin chains that mediate recognition by the proteasome. It is currently unclear how the proteasome recognizes its substrates, as the only established ubiquitin receptor intrinsic to the proteasome is Rpn10/S5a (ref. 1), which is not essential for ubiquitin-mediated protein degradation in budding yeast. In the accompanying manuscript we report that Rpn13 (refs 3-7), a component of the nine-subunit proteasome base, functions as a ubiquitin receptor, complementing its known role in docking de-ubiquitinating enzyme Uch37/UCHL5 (refs 4-6) to the proteasome. Here we merge crystallography and NMR data to describe the ubiquitin-binding mechanism of Rpn13. We determine the structure of Rpn13 alone and complexed with ubiquitin. The co-complex reveals a novel ubiquitin-binding mode in which loops rather than secondary structural elements are used to capture ubiquitin. Further support for the role of Rpn13 as a proteasomal ubiquitin receptor is demonstrated by its ability to bind ubiquitin and proteasome subunit Rpn2/S1 simultaneously. Finally, we provide a model structure of Rpn13 complexed to diubiquitin, which provides insights into how Rpn13 as a ubiquitin receptor is coupled to substrate deubiquitination by Uch37.
+
The line below this paragraph, {{ABSTRACT_PUBMED_18497827}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 18497827 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_18497827}}
==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Ubiquitin]]
[[Category: Ubiquitin]]
[[Category: Ubiquitin-proteasome-degradation pathway]]
[[Category: Ubiquitin-proteasome-degradation pathway]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 4 09:58:53 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 18:47:36 2008''

Revision as of 15:47, 27 July 2008

Image:2r2y.png

Template:STRUCTURE 2r2y

Crystal structure of the proteasomal Rpn13 PRU-domain

Template:ABSTRACT PUBMED 18497827

About this Structure

2R2Y is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

Ubiquitin docking at the proteasome through a novel pleckstrin-homology domain interaction., Schreiner P, Chen X, Husnjak K, Randles L, Zhang N, Elsasser S, Finley D, Dikic I, Walters KJ, Groll M, Nature. 2008 May 22;453(7194):548-52. PMID:18497827

Page seeded by OCA on Sun Jul 27 18:47:36 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2r2y"
Personal tools