Crystal structure of the protein from Arabidopsis thaliana gene At5g06450, a putative DnaQ‐like exonuclease domain‐containing protein with homohexameric assembly |
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| Authors: | David W Smith Mi Ra Han Joon Sung Park Kyung Rok Kim Taeho Yeom Ji Yeon Lee Do Jin Kim Craig A Bingman Hyun‐Jung Kim Kyubong Jo Byung Woo Han George N Phillips Jr |
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| Institution: | 1. Center for Eukaryotic Structural Genomics, Department of Biochemistry, University of Wisconsin‐Madison, , Madison, Wisconsin, 53706;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, Texas, 77251 |
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| 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.Proteins 2013. © 2013 Wiley Periodicals, Inc. |
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| Keywords: | 3′ ‐5′ exonuclease DnaQ‐like exonuclease family Arabidopsis thaliana AtDECP homohexamer crystal structure |
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