2nqh: Difference between revisions

Revision as of 20:35, 28 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:2nqh.png

Template:STRUCTURE 2nqh

High Resolution crystal structure of Escherichia coli endonuclease IV (Endo IV) E261Q mutantHigh Resolution crystal structure of Escherichia coli endonuclease IV (Endo IV) E261Q mutant

Template:ABSTRACT PUBMED 18408731

About this StructureAbout this Structure

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

ReferenceReference

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 Mon Jul 28 20:35:30 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:2nqh.jpg|left|200px]]
+{{Seed}}
+[[Image:2nqh.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2nqh|  PDB=2nqh  |  SCENE=  }}
-'''High Resolution crystal structure of Escherichia coli endonuclease IV (Endo IV) E261Q mutant'''
+===High Resolution crystal structure of Escherichia coli endonuclease IV (Endo IV) E261Q mutant===
-==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==
@@ Line 28: / Line 32: @@
 [[Category: Tim-barrel]]
 [[Category: Trinuclear zinc center]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 24 09:25:19 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:35:30 2008''