Premium
X‐ray crystal structure of Escherichia coli HspQ, a protein involved in the retardation of replication initiation
Author(s) -
Abe Yoshito,
Shioi Seijiro,
Kita Shunsuke,
Nakata Hikaru,
Maenaka Katsumi,
Kohda Daisuke,
Katayama Tsutomu,
Ueda Tadashi
Publication year - 2017
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12892
Subject(s) - trimer , escherichia coli , dna replication , crystal structure , chemistry , biology , replication (statistics) , crystallography , microbiology and biotechnology , genetics , biochemistry , dna , gene , dimer , virology , organic chemistry
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.