| Literature DB >> 14718656 |
Takuma Kasai1, 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 Matsuo, Kazutoshi Tani, Harukazu Suzuki, Takahiro Arakawa, Piero Carninci, Jun Kawai, Yoshihide Hayashizaki, Takanori Kigawa, Shigeyuki Yokoyama.
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 alphabetabetaalphaalphabetaalpha, in which beta(1) and beta(2) are antiparallel, and beta(3) is parallel to beta(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.Entities:
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Year: 2004 PMID： 14718656 PMCID： PMC2286707 DOI： 10.1110/ps.03401004
Source DB: PubMed Journal: Protein Sci ISSN： 0961-8368 Impact factor: 6.725