X-ray crystal structure of Escherichia coli HspQ, a protein involved in the retardation of replication initiation

FEBS Lett. 2017 Nov;591(22):3805-3816. doi: 10.1002/1873-3468.12892. Epub 2017 Nov 12.

Abstract

The heat shock protein HspQ (YccV) of Escherichia coli has been proposed to participate in the retardation of replication initiation in cells with the dnaA508 allele. In this study, we have determined the 2.5-Å-resolution X-ray structure of the trimer of HspQ, which is also the first structure of a member of the YccV superfamily. The acidic character of the HspQ trimer suggests an interaction surface with basic proteins. From these results, we discuss the cellular function of HspQ, including its relationship with the DnaA508 protein.

Keywords: DnaA; HspQ; crystal structure.

Publication types

  • Letter

MeSH terms

  • Crystallography, X-Ray
  • DNA Replication
  • DNA, Bacterial / metabolism*
  • Escherichia coli / chemistry
  • Escherichia coli / genetics
  • Escherichia coli / metabolism*
  • Escherichia coli Proteins / chemistry*
  • Escherichia coli Proteins / metabolism*
  • Heat-Shock Proteins / chemistry*
  • Heat-Shock Proteins / metabolism*
  • Models, Molecular
  • Protein Conformation
  • Protein Multimerization

Substances

  • DNA, Bacterial
  • Escherichia coli Proteins
  • Heat-Shock Proteins
  • HspQ protein, E coli