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.
| Original language | English |
|---|---|
| Pages (from-to) | 3805-3816 |
| Number of pages | 12 |
| Journal | FEBS Letters |
| Volume | 591 |
| Issue number | 22 |
| DOIs | |
| Publication status | Published - Nov 2017 |
All Science Journal Classification (ASJC) codes
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology
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