1M1G
Crystal Structure of Aquifex aeolicus N-utilization substance G (NusG), Space Group P2(1)
Summary for 1M1G
| Entry DOI | 10.2210/pdb1m1g/pdb |
| Descriptor | Transcription antitermination protein nusG (2 entities in total) |
| Functional Keywords | transcription termination, antitermination, kow domain, rnp motif, immunoglobulin fold, nucleic acid interaction, protein-protein interaction, transcription |
| Biological source | Aquifex aeolicus |
| Total number of polymer chains | 4 |
| Total formula weight | 112166.81 |
| Authors | Steiner, T.,Kaiser, J.T.,Marinkovic, S.,Huber, R.,Wahl, M.C. (deposition date: 2002-06-19, release date: 2003-02-04, Last modification date: 2024-10-30) |
| Primary citation | Steiner, T.,Kaiser, J.T.,Marinkovic, S.,Huber, R.,Wahl, M.C. Crystal structures of transcription factor NusG in light of its nucleic acid- and protein-binding activities Embo J., 21:4641-4653, 2002 Cited by PubMed Abstract: Microbial transcription modulator NusG interacts with RNA polymerase and termination factor rho, displaying striking functional homology to eukaryotic Spt5. The protein is also a translational regulator. We have determined crystal structures of Aquifex aeolicus NusG showing a modular design: an N-terminal RNP-like domain, a C-terminal element with a KOW sequence motif and a species-specific immunoglobulin-like fold. The structures reveal bona fide nucleic acid binding sites, and nucleic acid binding activities can be detected for NusG from three organisms and for the KOW element alone. A conserved KOW domain is defined as a new class of nucleic acid binding folds. This module is a close structural homolog of tudor protein-protein interaction motifs. Putative protein binding sites for the RNP and KOW domains can be deduced, which differ from the areas implicated in nucleic acid interactions. The results strongly argue that both protein and nucleic acid contacts are important for NusG's functions and that the factor can act as an adaptor mediating indirect protein-nucleic acid associations. PubMed: 12198166DOI: 10.1093/emboj/cdf455 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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