Solution structure of a BolA-like protein from Mus musculus

Takuma Kasai, Makoto Inoue, Seizo Koshiba, Takashi Yabuki, Masaaki Aoki, Emi Nunokawa, Eiko Seki, Takayoshi Matsuda, Natsuko Matsuda, Yasuko Tomo, Mikako Shirouzu, Takaho Terada, Naomi Obayashi, Hiroaki Hamana, Naoko Shinya, Ayako Tatsuguchi, Satoko Yasuda, Mayumi Yoshida, Hiroshi Hirota, Yo MatsuoKazutoshi Tani, Harukazu Suzuki, Takahiro Arakawa, Piero Carninci, Jun Kawai, Yoshihide Hayashizaki, Takanori Kigawa, Shigeyuki Yokoyama

Research output: Contribution to journalArticlepeer-review

40 Citations (Scopus)

Abstract

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 β1 and β2 are antiparallel, and β3 is parallel to β2. 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.

Original languageEnglish
Pages (from-to)545-548
Number of pages4
JournalProtein Science
Volume13
Issue number2
DOIs
Publication statusPublished - 2004 Feb

Keywords

  • BolA
  • Cell proliferation
  • Cell-cycle regulation
  • Conserved protein
  • KH fold
  • NMR structure
  • Structural genomics

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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