Structural highlights
Function
[HSPQ_ECO55] Involved in the degradation of certain denaturated proteins, including DnaA, during heat shock stress.
Publication Abstract from PubMed
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.
X-ray crystal structure of Escherichia coli HspQ, a protein involved in the retardation of replication initiation.,Abe Y, Shioi S, Kita S, Nakata H, Maenaka K, Kohda D, Katayama T, Ueda T FEBS Lett. 2017 Nov;591(22):3805-3816. doi: 10.1002/1873-3468.12892. Epub 2017, Nov 12. PMID:29083032[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Abe Y, Shioi S, Kita S, Nakata H, Maenaka K, Kohda D, Katayama T, Ueda T. 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. PMID:29083032 doi:http://dx.doi.org/10.1002/1873-3468.12892
