8WO8
Crystal Structure of an RNA-binding protein, FAU-1, from Pyrococcus furiosus
Summary for 8WO8
| Entry DOI | 10.2210/pdb8wo8/pdb |
| Descriptor | Probable ribonuclease FAU-1, RNA (5'-R(P*AP*UP*A)-3') (3 entities in total) |
| Functional Keywords | rnase e, rna binding protein |
| Biological source | Pyrococcus furiosus More |
| Total number of polymer chains | 2 |
| Total formula weight | 55957.73 |
| Authors | |
| Primary citation | Kawai, G.,Okada, K.,Baba, S.,Sato, A.,Sakamoto, T.,Kanai, A. Homo-trimeric structure of the ribonuclease for rRNA processing, FAU-1, from Pyrococcus furiosus. J.Biochem., 175:671-676, 2024 Cited by PubMed Abstract: Crystal structure of a ribonuclease for ribosomal RNA processing, FAU-1, from Pyrococcus furiosus was determined with the resolution of 2.57 Å in a homo-trimeric form. The monomer structure consists of two domains: N-terminal and C-terminal domains. C-terminal domain forms trimer and each N-terminal domain locates outside of the trimer core. In the obtained crystal, a dinucleotide, pApUp, was bound to the N-terminal domain, indicating that N-terminal domain has the RNA-binding ability. The affinities to RNA of FAU-1 and a fragment corresponding to the N-terminal domain, FAU-ΔC, were confirmed by polyacrylamide gel electrophoresis and nuclear magnetic resonance (NMR). Interestingly, well-dispersed NMR signals were observed at 318K, indicating that the FAU-ΔC-F18 complex form an ordered structure at higher temperature. As predicted in our previous works, FAU-1 and ribonuclease (RNase) E show a structural similarity in their RNA-binding regions. However, structural similarity between RNase E and FAU-1 could be found in the limited regions of the N-terminal domain. On the other hand, structural similarity between C-terminal domain and some proteins including a phosphatase was found. Thus, it is possible that the catalytic site is located in C-terminal domain. PubMed: 38302756DOI: 10.1093/jb/mvae010 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.78 Å) |
Structure validation
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