publication . Article . Other literature type . 2004

Solution structure of a BolA‐like protein from Mus musculus

Kasai, Takuma; Inoue, Makoto; Koshiba, Seizo; Yabuki, Takashi; Aoki, Masaaki; Nunokawa, Emi; Seki, Eiko; Matsuda, Takayoshi; Matsuda, Natsuko; Tomo, Yasuko; ...
Open Access
  • Published: 01 Feb 2004 Journal: Protein Science, volume 13, pages 545-548 (issn: 0961-8368, eissn: 1469-896X, Copyright policy)
  • Publisher: Wiley
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.
Subjects
free text keywords: Chemistry, Globin fold, Cell growth, Globular protein, chemistry.chemical_classification, Cell cycle, Peptide sequence, Thioredoxin fold, Biochemistry, Antiparallel (biochemistry), Structural genomics, For the Record
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