2z6o

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 4: Line 4:
==Overview==
==Overview==
-
Ubiquitin and ubiquitin-like protein-conjugating enzymes play central, roles in posttranslational modification processes. The ubiquitin-fold, modifier 1 (Ufm1), one of a variety of ubiquitin-like modifiers, is, covalently attached to target proteins via Uba5 and Ufm1-conjugating, enzyme 1 (Ufc1), which are analogous to the E1 and E2 ubiquitylation, enzymes. As Ufm1-related proteins are conserved in metazoa and plants, the, Ufm1 system likely plays important roles in various multicellular, organisms. Herein, we report the X-ray structure of human Ufc1 determined, at 1.6A resolution. The Ufc1 structure comprises a canonical E2 domain and, an additional N-terminal domain. The Uba5 binding site on Ufc1 was, assigned by structural comparison of Ufc1 and Ubc12 and related mutational, analyses. In addition, we show that the N-terminal unique domain of Ufc1, contributes to thermal stability.
+
Ubiquitin and ubiquitin-like protein-conjugating enzymes play central roles in posttranslational modification processes. The ubiquitin-fold modifier 1 (Ufm1), one of a variety of ubiquitin-like modifiers, is covalently attached to target proteins via Uba5 and Ufm1-conjugating enzyme 1 (Ufc1), which are analogous to the E1 and E2 ubiquitylation enzymes. As Ufm1-related proteins are conserved in metazoa and plants, the Ufm1 system likely plays important roles in various multicellular organisms. Herein, we report the X-ray structure of human Ufc1 determined at 1.6 A resolution. The Ufc1 structure comprises a canonical E2 domain and an additional N-terminal domain. The Uba5 binding site on Ufc1 was assigned by structural comparison of Ufc1 and Ubc12 and related mutational analyses. In addition, we show that the N-terminal unique domain of Ufc1 contributes to thermal stability.
==About this Structure==
==About this Structure==
Line 33: Line 33:
[[Category: ufm1]]
[[Category: ufm1]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 13:31:24 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:00:32 2008''

Revision as of 17:00, 21 February 2008

Image:2z6o.gif

2z6o, resolution 1.60Å

Drag the structure with the mouse to rotate

Crystal Structure of the Ufc1, Ufm1 conjugating enzyme 1

Overview

Ubiquitin and ubiquitin-like protein-conjugating enzymes play central roles in posttranslational modification processes. The ubiquitin-fold modifier 1 (Ufm1), one of a variety of ubiquitin-like modifiers, is covalently attached to target proteins via Uba5 and Ufm1-conjugating enzyme 1 (Ufc1), which are analogous to the E1 and E2 ubiquitylation enzymes. As Ufm1-related proteins are conserved in metazoa and plants, the Ufm1 system likely plays important roles in various multicellular organisms. Herein, we report the X-ray structure of human Ufc1 determined at 1.6 A resolution. The Ufc1 structure comprises a canonical E2 domain and an additional N-terminal domain. The Uba5 binding site on Ufc1 was assigned by structural comparison of Ufc1 and Ubc12 and related mutational analyses. In addition, we show that the N-terminal unique domain of Ufc1 contributes to thermal stability.

About this Structure

2Z6O is a Single protein structure of sequence from Homo sapiens with as ligand. Active as Ubiquitin--protein ligase, with EC number 6.3.2.19 Full crystallographic information is available from OCA.

Reference

Crystal structure of Ufc1, the Ufm1-conjugating enzyme., Mizushima T, Tatsumi K, Ozaki Y, Kawakami T, Suzuki A, Ogasahara K, Komatsu M, Kominami E, Tanaka K, Yamane T, Biochem Biophys Res Commun. 2007 Nov 3;362(4):1079-84. Epub 2007 Aug 30. PMID:17825256

Page seeded by OCA on Thu Feb 21 19:00:32 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2z6o"
Personal tools