Summary for 1V9J
Entry DOI | 10.2210/pdb1v9j/pdb |
Descriptor | BolA-like protein RIKEN cDNA 1110025L05 (1 entity in total) |
Functional Keywords | stationary phase morphogene, stress-induced morphogene, structural genomics, riken structural genomics/proteomics initiative, rsgi, unknown function |
Biological source | Mus musculus (house mouse) |
Total number of polymer chains | 1 |
Total formula weight | 12981.58 |
Authors | Kasai, T.,Inoue, M.,Koshiba, S.,Yabuki, T.,Aoki, M.,Nunokawa, E.,Seki, E.,Matsuda, T.,Matsuda, N.,Tomo, Y.,Shirouzu, M.,Terada, T.,Obayashi, N.,Hamana, H.,Shinya, N.,Tatsuguchi, A.,Yasuda, S.,Yoshida, M.,Hirota, H.,Matsuo, Y.,Tani, K.,Suzuki, H.,Arakawa, T.,Carninci, P.,Kawai, J.,Hayashizaki, Y.,Kigawa, T.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2004-01-26, release date: 2004-02-10, Last modification date: 2023-12-27) |
Primary citation | Kasai, T.,Inoue, M.,Koshiba, S.,Yabuki, T.,Aoki, M.,Nunokawa, E.,Seki, E.,Matsuda, T.,Matsuda, N.,Tomo, Y.,Shirouzu, M.,Terada, T.,Obayashi, N.,Hamana, H.,Shinya, N.,Tatsuguchi, A.,Yasuda, S.,Yoshida, M.,Hirota, H.,Matsuo, Y.,Tani, K.,Suzuki, H.,Arakawa, T.,Carninci, P.,Kawai, J.,Hayashizaki, Y.,Kigawa, T.,Yokoyama, S. Solution structure of a BolA-like protein from Mus musculus Protein Sci., 13:545-548, 2004 Cited by PubMed 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. PubMed: 14718656DOI: 10.1110/ps.03401004 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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