4ZN3
Crystal Structure of MjSpt4:Spt5 complex conformation B
Summary for 4ZN3
| Entry DOI | 10.2210/pdb4zn3/pdb |
| Related | 4ZN1 |
| Descriptor | Transcription elongation factor Spt5, Transcription elongation factor Spt4, GLYCEROL, ... (6 entities in total) |
| Functional Keywords | protein-protein complex, transcription |
| Biological source | Methanocaldococcus jannaschii DSM 2661 More |
| Total number of polymer chains | 2 |
| Total formula weight | 24595.53 |
| Authors | Guo, G.R.,Zhou, H.H.,Gao, Y.X.,Zhu, Z.L.,Niu, L.W.,Teng, M.K. (deposition date: 2015-05-04, release date: 2016-03-16, Last modification date: 2023-11-08) |
| Primary citation | Guo, G.R.,Gao, Y.X.,Zhu, Z.L.,Zhao, D.,Liu, Z.,Zhou, H.H.,Niu, L.W.,Teng, M.K. Structural and biochemical insights into the DNA-binding mode of MjSpt4p:Spt5 complex at the exit tunnel of RNAPII J.Struct.Biol., 192:418-425, 2015 Cited by PubMed Abstract: Spt5 (NusG in bacteria) is the only RNA polymerase-associated factor known to be conserved in all three domains of life. In archaea and eukaryotes, Spt5 associates with Spt4, an elongation factor that is absent in bacteria, to form a functional heterodimeric complex. Previous studies suggest that the Spt4:Spt5 complex interacts directly with DNA at the double-stranded DNA exit tunnel of RNA polymerase to regulate gene transcription. In this study, the DNA-binding ability of Spt4:Spt5 from the archaeon Methanocaldococcus jannaschii was confirmed via nuclear magnetic resonance chemical shift perturbation and fluorescence polarization assays. Crystallographic analysis of the full-length MjSpt4:Spt5 revealed two distinct conformations of the C-terminal KOW domain of Spt5. A similar alkaline region was found on the Spt4:Spt5 surface in both crystal forms, and identified as double-stranded DNA binding patch through mutagenesis-fluorescence polarization assays. Based on these structural and biochemical data, the Spt4:Spt5-DNA binding model was built for the first time. PubMed: 26433031DOI: 10.1016/j.jsb.2015.09.023 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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