X‐ray crystal structure of Escherichia coli HspQ, a protein involved in the retardation of replication initiation. Issue 22 (12th November 2017)

• Record Type: Journal Article
• Authors: Abe, Yoshito; Shioi, Seijiro; Kita, Shunsuke; Nakata, Hikaru; Maenaka, Katsumi; Kohda, Daisuke; Katayama, Tsutomu; Ueda, Tadashi
• Is Part Of: FEBS letters. Volume 591:Issue 22(2017)
• Page Start: 3805
• Page End: 3816
• Publication Date: 2017-11-12
• Subjects: crystal structure -- DnaA -- HspQ; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1002/1873-3468.12892
• Languages: English
• ISSNs: 0014-5793

Abstract

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. Abstract :