Format

Send to

Choose Destination
Proteins. 2013 Sep;81(9):1669-1675. 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, USA.
2
Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Seoul 151-742, Korea.
3
Department of Chemistry, Sogang University, Seoul 121-742, Korea.
4
College of Pharmacy, Chung-Ang University, Seoul 156-756, Korea.
5
Department of Biochemistry and Cell Biology, Rice University, Houston, TX 77251, USA.
#
Contributed equally

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

Supplemental Content

Full text links

Icon for Wiley Icon for PubMed Central
Loading ...
Support Center