5AFQ
Crystal structure of RPC62 - RPC32 beta
Summary for 5AFQ
| Entry DOI | 10.2210/pdb5afq/pdb |
| Descriptor | DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC3, RPC32 BETA (RPC7L) (2 entities in total) |
| Functional Keywords | replication, human rna polymerase iii |
| Biological source | HOMO SAPIENS (HUMAN) More |
| Cellular location | Nucleus : Q9BUI4 |
| Total number of polymer chains | 4 |
| Total formula weight | 158526.76 |
| Authors | Fribourg, S. (deposition date: 2015-01-23, release date: 2015-10-07, Last modification date: 2024-01-10) |
| Primary citation | Boissier, F.,Dumay-Odelot, H.,Teichmann, M.,Fribourg, S. Structural Analysis of Human Rpc32Beta - Rpc62 Complex. J.Struct.Biol., 192:313-, 2015 Cited by PubMed Abstract: Transcription initiation by eukaryotic RNA polymerase (Pol) III relies on the subcomplex RPC62/RPC39/RPC32. Two distinct isoforms of RPC32 are encoded in the human genome. RPC32α expression is highly regulated and found only in stem cells and transformed cells, whereas RPC32β is ubiquitously expressed in tissues. Here we identify a core-interacting domain of RPC32 sufficient for the interaction with RPC62. We present the crystal structure of a complex of RPC62 and the RPC32β core domain. RPC32β associates with the extended winged helix 1 and 2 and the coiled coil domain of RPC62 qualifying RPC32 as a molecular bridge in between RPC62 domains. The RPC62-RPC32 complex fit into EM data suggests a bi-functional role for RPC32 through interactions with the largest Pol III subunit and through solvent exposed residues. RPC32 positioning into Pol III suggests that subunit-specific contacts at the surface of the Pol III holoenzyme are critical for its function. PubMed: 26394183DOI: 10.1016/J.JSB.2015.09.004 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (7 Å) |
Structure validation
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