9KYK
Crystal structure of human TRIP4
Summary for 9KYK
| Entry DOI | 10.2210/pdb9kyk/pdb |
| Descriptor | Activating signal cointegrator 1, GLYCEROL (3 entities in total) |
| Functional Keywords | asch domain, dna binding protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 19839.75 |
| Authors | Guo, W.T.,Meng, C.Y.,Wen, Y.,Wu, B.X. (deposition date: 2024-12-09, release date: 2025-08-20, Last modification date: 2025-12-24) |
| Primary citation | Meng, C.,Shi, X.,Guo, W.,Jian, X.,Zhao, J.,Wen, Y.,Wang, R.,Li, Y.,Xu, S.,Chen, H.,Zhang, J.,Chen, M.,Chen, H.,Wu, B. Structural analysis of ASCH domain-containing proteins and their implications for nucleotide processing. Structure, 33:2095-2108.e5, 2025 Cited by PubMed Abstract: ASC-1 homology (ASCH) domain family proteins are believed to play essential roles in RNA metabolism, but detailed structural and functional information is limited. Research has shown that the E. coli enzyme YqfB, which contains an ASCH domain, has amidohydrolase activity, converting N-acetylcytidine (acC) RNA nucleoside into cytidine. Here, we present the crystal structures of EcYqfB both in its unbound state and bound to a substrate. Our analysis reveals how the substrate interacts with the enzyme, offering insights into its catalytic mechanism. In vivo experiments further show that deleting EcYqfB does not change overall acC levels across various RNA types, indicating that EcYqfB specifically functions in acC nucleoside metabolism. We also determined the structures of two homologous proteins: mouse EOLA1 and the human TRIP4-ASCH domain, highlighting differences in their substrate preferences. These findings offer important insights for future research into the structure and function of the ASCH domain protein family. PubMed: 40939588DOI: 10.1016/j.str.2025.08.015 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.02 Å) |
Structure validation
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