2CXC
Crystal structure of archaeal transcription termination factor NusA
Summary for 2CXC
| Entry DOI | 10.2210/pdb2cxc/pdb |
| Descriptor | NusA (2 entities in total) |
| Functional Keywords | transcription termination, rna binding protein, archaeal nusa, kh domain, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, transcription |
| Biological source | Aeropyrum pernix |
| Total number of polymer chains | 1 |
| Total formula weight | 16069.72 |
| Authors | Shibata, R.,Bessho, Y.,Shirouzu, M.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2005-06-28, release date: 2005-12-28, Last modification date: 2024-03-13) |
| Primary citation | Shibata, R.,Bessho, Y.,Shinkai, A.,Nishimoto, M.,Fusatomi, E.,Terada, T.,Shirouzu, M.,Yokoyama, S. Crystal structure and RNA-binding analysis of the archaeal transcription factor NusA Biochem.Biophys.Res.Commun., 355:122-128, 2007 Cited by PubMed Abstract: The transcription factor NusA functions in transcriptional regulation involving termination in bacteria. A NusA homolog consisting of only the two KH domains is widely conserved in archaea, but its function remains unknown. We have found that Aeropyrum pernix NusA strongly binds to a certain CU-rich sequence near a termination signal. Our crystal structure of A. pernix NusA revealed that its spatial arrangement is quite similar to that of the KH domains of bacterial NusA. Thus, we consider archaeal NusA to have retained some functions of bacterial NusA, including the ssRNA-binding ability. Remarkable structural differences between archaeal and bacterial NusA exist at the interface with RNAP, in connection with the different NusA-binding sites around the termination signals. Transcriptional termination in archaea could differ from all of the known bacterial and eukaryal mechanisms, in terms of the combination of a bacterial factor and a eukaryal-type RNAP. PubMed: 17288993DOI: 10.1016/j.bbrc.2007.01.119 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
Download full validation report
