2XV4
Structure of Human RPC62 (partial)
Summary for 2XV4
| Entry DOI | 10.2210/pdb2xv4/pdb |
| Related | 2XUB |
| Descriptor | DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC3, PHOSPHATE ION (3 entities in total) |
| Functional Keywords | transcription, winged helix |
| Biological source | HOMO SAPIENS (HUMAN) |
| Cellular location | Nucleus (By similarity): Q9BUI4 |
| Total number of polymer chains | 1 |
| Total formula weight | 60977.47 |
| Authors | Lefevre, S.,Legrand, P.,Fribourg, S. (deposition date: 2010-10-22, release date: 2011-03-02, Last modification date: 2024-05-08) |
| Primary citation | Lefevre, S.,Dumay-Odelot, H.,El Ayoubi, L.,Budd, A.,Legrand, P.,Pinaud, N.,Teichmann, M.,Fribourg, S. Structure-Function Analysis of Hrpc62 Provides Insights Into RNA Polymerase III Transcription Nat.Struct.Mol.Biol., 18:352-, 2011 Cited by PubMed Abstract: The 17-subunit human RNA polymerase III (hPol III) transcribes small, untranslated RNA genes that are involved in the regulation of transcription, splicing and translation. hPol III subunits hRPC62, hRPC39 and hRPC32 form a stable ternary subcomplex required for promoter-specific transcription initiation by hPol III. Here, we report the crystal structure of hRPC62. This subunit folds as a four-tandem extended winged helix (eWH) protein that is structurally related to the transcription factor TFIIEα N terminus. Through biochemical analyses, we mapped the protein-protein interactions of hRPC62, hRPC32 and hRPC39. In addition, we demonstrated that hRPC62 and hRPC39 bind single-stranded and duplex DNA, respectively, in a sequence-independent manner. Overall, we shed light on structural similarities between the hPol III-specific subunit hRPC62 and TFIIEα and propose specific functions for hRPC39 and hRPC62 in transcription initiation by hPol III. PubMed: 21358628DOI: 10.1038/NSMB.1996 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.95 Å) |
Structure validation
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