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Solution structure of a BolA‐like protein from Mus musculus
Author(s) -
Kasai Takuma,
Inoue Makoto,
Koshiba Seizo,
Yabuki Takashi,
Aoki Masaaki,
Nunokawa Emi,
Seki Eiko,
Matsuda Takayoshi,
Matsuda Natsuko,
Tomo Yasuko,
Shirouzu Mikako,
Terada Takaho,
Obayashi Naomi,
Hamana Hiroaki,
Shinya Naoko,
Tatsuguchi Ayako,
Yasuda Satoko,
Yoshida Mayumi,
Hirota Hiroshi,
Matsuo Yo,
Tani Kazutoshi,
Suzuki Harukazu,
Arakawa Takahiro,
Carninci Piero,
Kawai Jun,
Hayashizaki Yoshihide,
Kigawa Takanori,
Yokoyama Shigeyuki
Publication year - 2004
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.03401004
Subject(s) - antiparallel (mathematics) , conserved sequence , biology , beta (programming language) , protein structure , microbiology and biotechnology , genetics , peptide sequence , gene , physics , biochemistry , quantum mechanics , magnetic field , computer science , programming language
The BolA‐like proteins are widely conserved from prokaryotes to eukaryotes. The BolA‐like proteins seem to be involved in cell proliferation or cell‐cycle regulation, but the molecular function is still unknown. Here we determined the structure of a mouse BolA‐like protein. The overall topology is αββααβα, in which β 1 and β 2 are antiparallel, and β 3 is parallel to β 2 . This fold is similar to the class II KH fold, except for the absence of the GXXG loop, which is well conserved in the KH fold. The conserved residues in the BolA‐like proteins are assembled on the one side of the protein.