2nq9: Difference between revisions

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[[Image:2nq9.gif|left|200px]]
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{{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==
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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.
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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 zn active site]]
[[Category: Trinuclear zn active site]]
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