2z6p: Difference between revisions

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==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==

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[[Category: ufm1]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:00:33 2008''

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@@ Line 4: / Line 4: @@
 ==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==
@@ Line 32: / Line 32: @@
 [[Category: ufm1]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 13:31:25 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:00:33 2008''