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Proteins. 2013 Sep;81(9):1669-75. doi: 10.1002/prot.24315. Epub 2013 Jun 17.

Crystal structure of the protein from Arabidopsis thaliana gene At5g06450, a putative DnaQ-like exonuclease domain-containing protein with homohexameric assembly.

Author information

1
Center for Eukaryotic Structural Genomics, Department of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin, 53706.

Abstract

Arabidopsis thaliana gene At5g06450 encodes a putative DnaQ-like 3'-5' exonuclease domain-containing protein (AtDECP). The DnaQ-like 3'-5' exonuclease domain is often found as a proofreading domain of DNA polymerases. The overall structure of AtDECP adopts an RNase H fold that consists of a mixed β-sheet flanked by α-helices. Interestingly, AtDECP forms a homohexameric assembly with a central six fold symmetry, generating a central cavity. The ring-shaped structure and comparison with WRN-exo, the best structural homologue of AtDECP, suggest a possible mechanism for implementing its exonuclease activity using positively charged patch on the N-terminal side of the homohexameric assembly. The homohexameric structure of AtDECP provides unique information about the interaction between the DnaQ-like 3'-5' exonuclease and its substrate nucleic acids.

KEYWORDS:

3′-5′ exonuclease; Arabidopsis thaliana; AtDECP; DnaQ-like exonuclease family; crystal structure; homohexamer

PMID:
23616405
PMCID:
PMC4435538
DOI:
10.1002/prot.24315
[Indexed for MEDLINE]
Free PMC Article
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