2DFH
Crystal structure of Tk-RNase HII(1-212)-C
Summary for 2DFH
Entry DOI | 10.2210/pdb2dfh/pdb |
Related | 1IO2 2DFE 2DFF 2DFG |
Descriptor | Ribonuclease HII (2 entities in total) |
Functional Keywords | chameleon sequence, ribonuclease hii, thermococcus kodakaraensis, fusion protein, hydrolase |
Biological source | Thermococcus kodakarensis |
Cellular location | Cytoplasm (Potential): O74035 |
Total number of polymer chains | 1 |
Total formula weight | 24865.41 |
Authors | Katagiri, Y.,Takano, K.,Chon, H.,Matsumura, H.,Koga, Y.,Kanaya, S. (deposition date: 2006-03-01, release date: 2007-03-06, Last modification date: 2023-10-25) |
Primary citation | Takano, K.,Katagiri, Y.,Mukaiyama, A.,Chon, H.,Matsumura, H.,Koga, Y.,Kanaya, S. Conformational contagion in a protein: Structural properties of a chameleon sequence Proteins, 68:617-625, 2007 Cited by PubMed Abstract: Certain sequences, known as chameleon sequences, take both alpha- and beta-conformations in natural proteins. We demonstrate that a wild chameleon sequence fused to the C-terminal alpha-helix or beta-sheet in foreign stable proteins from hyperthermophiles forms the same conformation as the host secondary structure. However, no secondary structural formation is observed when the sequence is attached to the outside of the secondary structure. These results indicate that this sequence inherently possesses an ability to make either alpha- or beta-conformation, depending on the sequentially neighboring secondary structure if little other nonlocal interaction occurs. Thus, chameleon sequences take on a satellite state through contagion by the power of a secondary structure. We propose this "conformational contagion" as a new nonlocal determinant factor in protein structure and misfolding related to protein conformational diseases. PubMed: 17510955DOI: 10.1002/prot.21451 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.27 Å) |
Structure validation
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