Crystal structure of the winged-helix domain of MCM8

Huan Zeng; Jun Li; Huiqin Xu; Huanhuan Li; Yingfang Liu

doi:10.1016/j.bbrc.2020.03.150

Crystal structure of the winged-helix domain of MCM8

Biochem Biophys Res Commun. 2020 Jun 11;526(4):993-998. doi: 10.1016/j.bbrc.2020.03.150. Epub 2020 Apr 12.

Authors

Huan Zeng¹, Jun Li¹, Huiqin Xu¹, Huanhuan Li², Yingfang Liu³

Affiliations

¹ School of Medicine, Sun Yat-Sen University, Guangzhou, 510275, China.
² Guangdong Provincial Key Laboratory of Colorectal and Pelvic Floor Diseases, The Sixth Affiliated Hospital, Guangzhou, 510275, China.
³ Guangdong Provincial Key Laboratory of Colorectal and Pelvic Floor Diseases, The Sixth Affiliated Hospital, School of Medicine, Sun Yat-Sen University, Guangzhou, 510275, China. Electronic address: liuyingf5@mail.sysu.edu.cn.

PMID: 32295713
DOI: 10.1016/j.bbrc.2020.03.150

Abstract

Minichromosome maintenance 8 (MCM8) is a recently identified member of the minichromosome maintenance family, which possesses helicase and ATPase activity. It interacts with MCM9 and participates in homologous recombination repair. The structure of MCM8 is unclear now. Here, we report the crystal structure of the winged-helix domain of human MCM8 (MCM8-WHD) at 1.21 Å resolution. MCM8-WHD adopts a conserved winged-helix architecture. Structure analysis and biochemical study results showed the DNA binding ability and crucial residues of MCM8-WHD. Our results are helpful to understand the function of MCM8.

Keywords: Crystal structure; Helicase; MCM8; Winged-helix domain.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Crystallography, X-Ray
DNA / chemistry
HEK293 Cells
Humans
Minichromosome Maintenance Proteins / chemistry*
Models, Molecular
Protein Binding
Protein Domains
RecQ Helicases / chemistry

Substances

DNA
MCM8 protein, human
Minichromosome Maintenance Proteins
RecQ Helicases