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X-ray crystal structure of Escherichia coli HspQ, a protein involved in the retardation of replication initiation
- Source :
- FEBS letters. 591(22)
- Publication Year :
- 2017
-
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-A-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. This article is protected by copyright. All rights reserved.
- Subjects :
- 0301 basic medicine
DNA Replication
DNA, Bacterial
Models, Molecular
Protein Conformation
Biophysics
Trimer
Crystal structure
Biology
medicine.disease_cause
Crystallography, X-Ray
Biochemistry
DNA-binding protein
03 medical and health sciences
Structural Biology
Heat shock protein
Genetics
medicine
Escherichia coli
Molecular Biology
Heat-Shock Proteins
030102 biochemistry & molecular biology
Escherichia coli Proteins
Cell Biology
DnaA
030104 developmental biology
Replication Initiation
Protein Multimerization
Function (biology)
Subjects
Details
- ISSN :
- 18733468
- Volume :
- 591
- Issue :
- 22
- Database :
- OpenAIRE
- Journal :
- FEBS letters
- Accession number :
- edsair.doi.dedup.....380dffb1c6517b567ee22f72493d066d