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Structure of an aprataxin-DNA complex with insights into AOA1 neurodegenerative disease.

Abstract：

:DNA ligases finalize DNA replication and repair through DNA nick-sealing reactions that can abort to generate cytotoxic 5'-adenylation DNA damage. Aprataxin (Aptx) catalyzes direct reversal of 5'-adenylate adducts to protect genome integrity. Here the structure of a Schizosaccharomyces pombe Aptx-DNA-AMP-Zn(2+) complex reveals active site and DNA interaction clefts formed by fusing a histidine triad (HIT) nucleotide hydrolase with a DNA minor groove-binding C(2)HE zinc finger (Znf). An Aptx helical 'wedge' interrogates the base stack for sensing DNA ends or DNA nicks. The HIT-Znf, the wedge and an '[F/Y]PK' pivot motif cooperate to distort terminal DNA base-pairing and direct 5'-adenylate into the active site pocket. Structural and mutational data support a wedge-pivot-cut HIT-Znf catalytic mechanism for 5'-adenylate adduct recognition and removal and suggest that mutations affecting protein folding, the active site pocket and the pivot motif underlie Aptx dysfunction in the neurodegenerative disorder ataxia with oculomotor apraxia 1 (AOA1).

journal_name

Nat Struct Mol Biol

journal_title

Nature structural & molecular biology

authors

Tumbale P,Appel CD,Kraehenbuehl R,Robertson PD,Williams JS,Krahn J,Ahel I,Williams RS

doi

10.1038/nsmb.2146

subject

Has Abstract

pub_date

2011-10-09 00:00:00

pages

1189-95

issue

11

eissn

1545-9993

issn

1545-9985

pii

nsmb.2146

journal_volume

18

pub_type

杂志文章

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