2nqj: Difference between revisions

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[[Image:2nqj.gif|left|200px]]
{{Seed}}
[[Image:2nqj.png|left|200px]]


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{{STRUCTURE_2nqj|  PDB=2nqj  |  SCENE=  }}  
{{STRUCTURE_2nqj|  PDB=2nqj  |  SCENE=  }}  


'''Crystal structure of Escherichia coli endonuclease IV (Endo IV) E261Q mutant bound to damaged DNA'''
===Crystal structure of Escherichia coli endonuclease IV (Endo IV) E261Q mutant bound to damaged DNA===




==Overview==
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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.
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{{ABSTRACT_PUBMED_18408731}}


==About this Structure==
==About this Structure==
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[[Category: Tim_barrel]]
[[Category: Tim_barrel]]
[[Category: Trinuclear zinc site]]
[[Category: Trinuclear zinc site]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 24 09:25:20 2008''
 
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