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.


1m08

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1m08.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1m08.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1m08| PDB=1m08 | SCENE= }}
{{STRUCTURE_1m08| PDB=1m08 | SCENE= }}
-
'''Crystal structure of the unbound nuclease domain of ColE7'''
+
===Crystal structure of the unbound nuclease domain of ColE7===
-
==Overview==
+
<!--
-
The bacterial toxin ColE7 contains an H-N-H endonuclease domain (nuclease ColE7) that digests cellular DNA or RNA non-specifically in target cells, leading to cell death. In the host cell, protein Im7 forms a complex with ColE7 to inhibit its nuclease activity. Here, we present the crystal structure of the unbound nuclease ColE7 at a resolution of 2.1A. Structural comparison between the unbound and bound nuclease ColE7 in complex with Im7, suggests that Im7 is not an allosteric inhibitor that induces backbone conformational changes in nuclease ColE7, but rather one that inhibits by blocking the substrate-binding site. There were two nuclease ColE7 molecules in the P1 unit cell in crystals and they appeared as a dimer related to each other by a non-crystallographic dyad symmetry. Gel-filtration and cross-linking experiments confirmed that nuclease ColE7 indeed formed dimers in solution and that the dimeric conformation was more favored in the presence of double-stranded DNA. Structural comparison of nuclease ColE7 with the His-Cys box homing endonuclease I-PpoI further demonstrated that H-N-H motifs in dimeric nuclease ColE7 were oriented in a manner very similar to that of the betabetaalpha-fold of the active sites found in dimeric I-PpoI. A mechanism for the binding of double-stranded DNA by dimeric H-N-H nuclease ColE7 is suggested.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12441102}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12441102 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12441102}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Hnh motif]]
[[Category: Hnh motif]]
[[Category: Zn-binding protein]]
[[Category: Zn-binding protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:28:42 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 22:55:50 2008''

Revision as of 19:55, 2 July 2008

Image:1m08.png

Template:STRUCTURE 1m08

Crystal structure of the unbound nuclease domain of ColE7

Template:ABSTRACT PUBMED 12441102

About this Structure

1M08 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

The crystal structure of the nuclease domain of colicin E7 suggests a mechanism for binding to double-stranded DNA by the H-N-H endonucleases., Cheng YS, Hsia KC, Doudeva LG, Chak KF, Yuan HS, J Mol Biol. 2002 Nov 22;324(2):227-36. PMID:12441102

Page seeded by OCA on Wed Jul 2 22:55:50 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1m08"
Personal tools