1I4W
THE CRYSTAL STRUCTURE OF THE TRANSCRIPTION FACTOR SC-MTTFB OFFERS INTRIGUING INSIGHTS INTO MITOCHONDRIAL TRANSCRIPTION
Summary for 1I4W
| Entry DOI | 10.2210/pdb1i4w/pdb |
| Descriptor | MITOCHONDRIAL REPLICATION PROTEIN MTF1, XENON (3 entities in total) |
| Functional Keywords | mitochondrial transcription factor, transcription initiation, transcription |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Total number of polymer chains | 1 |
| Total formula weight | 41488.03 |
| Authors | Schubot, F.D.,Chen, C.-J.,Rose, J.P.,Dailey, T.A.,Dailey, H.A.,Wang, B.-C. (deposition date: 2001-02-23, release date: 2001-10-03, Last modification date: 2024-02-07) |
| Primary citation | Schubot, F.D.,Chen, C.J.,Rose, J.P.,Dailey, T.A.,Dailey, H.A.,Wang, B.C. Crystal structure of the transcription factor sc-mtTFB offers insights into mitochondrial transcription. Protein Sci., 10:1980-1988, 2001 Cited by PubMed Abstract: Although it is commonly accepted that binding of mitochondrial transcription factor sc-mtTFB to the mitochondrial RNA polymerase is required for specific transcription initiation in Saccharomyces cerevisiae, its precise role has remained undefined. In the present work, the crystal structure of sc-mtTFB has been determined to 2.6 A resolution. The protein consists of two domains, an N-terminal alpha/beta-domain and a smaller domain made up of four alpha-helices. Contrary to previous predictions, sc-mtTFB does not resemble Escherichia coli sigma-factors but rather is structurally homologous to rRNA methyltransferase ErmC'. This suggests that sc-mtTFB functions as an RNA-binding protein, an observation standing in contradiction to the existing model, which proposed a direct interaction of sc-mtTFB with the mitochondrial DNA promoter. Based on the structure, we propose that the promoter specificity region is located on the mitochondrial RNA polymerase and that binding of sc-mtTFB indirectly mediates interaction of the core enzyme with the promoter site. PubMed: 11567089DOI: 10.1110/ps.11201 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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