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.


1e44

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1e44.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1e44.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1e44| PDB=1e44 | SCENE= }}
{{STRUCTURE_1e44| PDB=1e44 | SCENE= }}
-
'''RIBONUCLEASE DOMAIN OF COLICIN E3 IN COMPLEX WITH ITS IMMUNITY PROTEIN'''
+
===RIBONUCLEASE DOMAIN OF COLICIN E3 IN COMPLEX WITH ITS IMMUNITY PROTEIN===
-
==Overview==
+
<!--
-
BACKGROUND: The cytotoxicity of most ribonuclease E colicins towards Escherichia coli arises from their ability to specifically cleave between bases 1493 and 1494 of 16S ribosomal RNA. This activity is carried by the C-terminal domain of the colicin, an activity which if left unneutralised would lead to destruction of the producing cell. To combat this the host E. coli cell produces an inhibitor protein, the immunity protein, which forms a complex with the ribonuclease domain effectively suppressing its activity. RESULTS: We have solved the crystal structure of the cytotoxic domain of the ribonuclease colicin E3 in complex with its immunity protein, Im3. The structure of the ribonuclease domain, the first of its class, reveals a highly twisted central beta-sheet elaborated with a short N-terminal helix, the residues of which form a well-packed interface with the immunity protein. CONCLUSIONS: The structure of the ribonuclease domain of colicin E3 is novel and forms an interface with its inhibitor which is significantly different in character to that reported for the DNase colicin complexes with their immunity proteins. The structure also gives insight into the mode of action of this class of enzymatic colicins by allowing the identification of potentially catalytic residues. This in turn reveals that the inhibitor does not bind at the active site but rather at an adjacent site, leaving the catalytic centre exposed in a fashion similar to that observed for the DNase colicins. Thus, E. coli appears to have evolved similar methods for ensuring efficient inhibition of the potentially destructive effects of the two classes of enzymatic colicins.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10986462}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10986462 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10986462}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Ribosome inactivation]]
[[Category: Ribosome inactivation]]
[[Category: Toxin]]
[[Category: Toxin]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:38:25 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:07:15 2008''

Revision as of 21:07, 30 June 2008

Image:1e44.png

Template:STRUCTURE 1e44

RIBONUCLEASE DOMAIN OF COLICIN E3 IN COMPLEX WITH ITS IMMUNITY PROTEIN

Template:ABSTRACT PUBMED 10986462

About this Structure

1E44 is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Inhibition of a ribosome-inactivating ribonuclease: the crystal structure of the cytotoxic domain of colicin E3 in complex with its immunity protein., Carr S, Walker D, James R, Kleanthous C, Hemmings AM, Structure. 2000 Sep 15;8(9):949-60. PMID:10986462

Page seeded by OCA on Tue Jul 1 00:07:15 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1e44"
Personal tools