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X-ray crystal structure of Escherichia coli HspQ, a protein involved in the retardation of replication initiation. 2017
Yoshito Abe, and
Seijiro Shioi, and
Shunsuke Kita, and
Hikaru Nakata, and
Katsumi Maenaka, and
Daisuke Kohda, and
Tsutomu Katayama, and
Tadashi Ueda
Department of Protein Structure, Function and Design, Graduate School of Pharmaceutical Sciences, Kyushu University, Fukuoka, Japan.
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.
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