2e2c: Difference between revisions

Revision as of 23:34, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2e2c.png

Template:STRUCTURE 2e2c

E2-C, AN UBIQUITIN CONJUGATING ENZYME REQUIRED FOR THE DESTRUCTION OF MITOTIC CYCLINSE2-C, AN UBIQUITIN CONJUGATING ENZYME REQUIRED FOR THE DESTRUCTION OF MITOTIC CYCLINS

Template:ABSTRACT PUBMED 10350465

About this StructureAbout this Structure

2E2C is a Single protein structure of sequence from Spisula solidissima. This structure supersedes the now removed PDB entry 1e2c. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the cyclin-specific ubiquitin-conjugating enzyme from clam, E2-C, at 2.0 A resolution., Jiang F, Basavappa R, Biochemistry. 1999 May 18;38(20):6471-8. PMID:10350465

Page seeded by OCA on Sun Jul 27 23:34:47 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:2e2c.gif|left|200px]]
+{{Seed}}
+[[Image:2e2c.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2e2c|  PDB=2e2c  |  SCENE=  }}
-'''E2-C, AN UBIQUITIN CONJUGATING ENZYME REQUIRED FOR THE DESTRUCTION OF MITOTIC CYCLINS'''
+===E2-C, AN UBIQUITIN CONJUGATING ENZYME REQUIRED FOR THE DESTRUCTION OF MITOTIC CYCLINS===
-==Overview==
+<!--
-The destruction of the cyclin B protein is necessary for the cell to exit from mitosis. The destruction of cyclin B occurs via the ubiquitin/proteasome system and involves a specific ubiquitin-conjugating enzyme (Ubc) that donates ubiquitin to cyclin B. Here we present the crystal structure of the cyclin-specific Ubc from clam, E2-C, determined at 2.0 A resolution. The E2-C enzyme contains an N-terminal extension in addition to the Ubc core domain. The N-terminal extension is disordered, perhaps reflecting a need for flexibility as it interacts with various partners in the ubiquitination system. The overall structure of the E2-C core domain is quite similar to those in previously determined Ubc proteins. The interaction between particular pairs of E2-C proteins in the crystal has some of the hallmarks of a functional dimer, though solution studies suggest that the E2-C protein exists as a monomer. Comparison of the E2-C structure with that of the other available Ubc structures indicates conserved surface residues that may interact with common components of the ubiquitination system. Such comparison also reveals a remarkable spine of conserved hydrophobic residues in the center of the protein that may drive the protein to fold and stabilize the protein once folded. Comparison of residues conserved only among E2-C and its homologues indicates surface areas that may be involved in mitotic-specific ubiquitination.
+The line below this paragraph, {{ABSTRACT_PUBMED_10350465}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10350465 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10350465}}
 ==About this Structure==
@@ Line 29: / Line 33: @@
 [[Category: Ubiquitin carrier protein]]
 [[Category: Ubiquitin conjugation]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 01:47:22 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:34:47 2008''