2Z8U
Methanococcus jannaschii TBP
Summary for 2Z8U
| Entry DOI | 10.2210/pdb2z8u/pdb |
| Descriptor | TATA-box-binding protein (2 entities in total) |
| Functional Keywords | transcription, dna-binding protein, transcription factor, transcription regulation |
| Biological source | Methanococcus jannaschii |
| Total number of polymer chains | 4 |
| Total formula weight | 83757.16 |
| Authors | Adachi, N.,Senda, T.,Horikoshi, M. (deposition date: 2007-09-10, release date: 2008-08-26, Last modification date: 2023-11-01) |
| Primary citation | Adachi, N.,Senda, M.,Natsume, R.,Senda, T.,Horikoshi, M. Crystal structure of Methanococcus jannaschii TATA box-binding protein. Genes Cells, 13:1127-1140, 2008 Cited by PubMed Abstract: As the archaeal transcription system consists of a eukaryotic-type transcription apparatus and bacterial-type regulatory transcription factors, analyses of the molecular interface between the transcription apparatus and regulatory transcription factors are critical to reveal the evolutionary change of the transcription system. TATA box-binding protein (TBP), the central components of the transcription apparatus are classified into three groups: eukaryotic, archaeal-I and archaeal-II TBPs. Thus, comparative functional analysis of these three groups of TBP is important for the study of the evolution of the transcription system. Here, we present the first crystal structure of an archaeal-II TBP from Methanococcus jannaschii. The highly conserved and group-specific conserved surfaces of TBP bind to DNA and TFIIB/TFB, respectively. The phylogenetic trees of TBP and TFIIB/TFB revealed that they evolved in a coupled manner. The diversified surface of TBP is negatively charged in the archaeal-II TBP, which is completely different from the case of eukaryotic and archaeal-I TBPs, which are positively charged and biphasic, respectively. This difference is responsible for the diversification of the regulatory functions of TBP during evolution. PubMed: 19090808DOI: 10.1111/j.1365-2443.2008.01233.x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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