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.


2nq9

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2nq9.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2nq9.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2nq9| PDB=2nq9 | SCENE= }}
{{STRUCTURE_2nq9| PDB=2nq9 | SCENE= }}
-
'''High resolution crystal structure of Escherichia coli endonuclease IV (Endo IV) Y72A mutant bound to damaged DNA'''
+
===High resolution crystal structure of Escherichia coli endonuclease IV (Endo IV) Y72A mutant bound to damaged DNA===
-
==Overview==
+
<!--
-
Escherichia coli endonuclease IV is an archetype for an abasic or apurinic-apyrimidinic endonuclease superfamily crucial for DNA base excision repair. Here biochemical, mutational and crystallographic characterizations reveal a three-metal ion mechanism for damage binding and incision. The 1.10-A resolution DNA-free and the 2.45-A resolution DNA-substrate complex structures capture substrate stabilization by Arg37 and reveal a distorted Zn(3)-ligand arrangement that reverts, after catalysis, to an ideal geometry suitable to hold rather than release cleaved DNA product. The 1.45-A resolution DNA-product complex structure shows how Tyr72 caps the active site, tunes its dielectric environment and promotes catalysis by Glu261-activated hydroxide, bound to two Zn(2+) ions throughout catalysis. These structural, mutagenesis and biochemical results suggest general requirements for abasic site removal in contrast to features specific to the distinct endonuclease IV alpha-beta triose phosphate isomerase (TIM) barrel and APE1 four-layer alpha-beta folds of the apurinic-apyrimidinic endonuclease families.
+
The line below this paragraph, {{ABSTRACT_PUBMED_18408731}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 18408731 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_18408731}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Tim-barrel]]
[[Category: Tim-barrel]]
[[Category: Trinuclear zn active site]]
[[Category: Trinuclear zn active site]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 24 09:25:13 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:26:30 2008''

Revision as of 04:26, 29 July 2008

Template:STRUCTURE 2nq9

High resolution crystal structure of Escherichia coli endonuclease IV (Endo IV) Y72A mutant bound to damaged DNA

Template:ABSTRACT PUBMED 18408731

About this Structure

2NQ9 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

DNA apurinic-apyrimidinic site binding and excision by endonuclease IV., Garcin ED, Hosfield DJ, Desai SA, Haas BJ, Bjoras M, Cunningham RP, Tainer JA, Nat Struct Mol Biol. 2008 Apr 13;. PMID:18408731

Page seeded by OCA on Tue Jul 29 07:26:30 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools