1NZ9
Solution Structure of the N-utilization substance G (NusG) C-terminal (NGC) domain from Thermus thermophilus
Summary for 1NZ9
| Entry DOI | 10.2210/pdb1nz9/pdb |
| Related | 1NZ8 |
| Descriptor | TRANSCRIPTION ANTITERMINATION PROTEIN NUSG (1 entity in total) |
| Functional Keywords | transcription elongation, termination, antitermination, riken structural genomics/proteomics initiative, rsgi, structural genomics, transcription |
| Biological source | Thermus thermophilus |
| Total number of polymer chains | 1 |
| Total formula weight | 6361.22 |
| Authors | Reay, P.,Yamasaki, K.,Terada, T.,Kuramitsu, S.,Shirouzu, M.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2003-02-17, release date: 2004-04-06, Last modification date: 2024-05-29) |
| Primary citation | Reay, P.,Yamasaki, K.,Terada, T.,Kuramitsu, S.,Shirouzu, M.,Yokoyama, S. Structural and sequence comparisons arising from the solution structure of the transcription elongation factor NusG from Thermus thermophilus Proteins, 56:40-51, 2004 Cited by PubMed Abstract: NusG is an essential bacterial protein modulator of transcriptional elongation and termination events, and interacts directly with RNA polymerase and Rho protein. Found also in Archaea, NusG shows stretches of sequence similarity to the eukaryotic transcription elongation factor Spt5. Herein, the three-dimensional solution structure of the bacterial NusG from Thermus thermophilus, which shows 43% amino acid sequence similarity to the Escherichia coli NusG, is described, and a survey of NusG and Spt5 amino acid sequences is presented. Although there is a clear evolutionary and functional relationship between these proteins, it is evident from the structural, sequence, and biochemical data that their binding specificities to both nucleic acids and other proteins differ. PubMed: 15162485DOI: 10.1002/prot.20054 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
