Summary for 1Z60
| Entry DOI | 10.2210/pdb1z60/pdb |
| Descriptor | TFIIH basal transcription factor complex p44 subunit, ZINC ION (2 entities in total) |
| Functional Keywords | basic transcription factor, zinc binding protein, ring finger, transcription |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus: Q13888 |
| Total number of polymer chains | 1 |
| Total formula weight | 6826.35 |
| Authors | Kellenberger, E.,Dominguez, C.,Fribourg, S.,Wasielewski, E.,Moras, D.,Poterszman, A.,Boelens, R.,Kieffer, B. (deposition date: 2005-03-21, release date: 2005-04-12, Last modification date: 2024-05-29) |
| Primary citation | Kellenberger, E.,Dominguez, C.,Fribourg, S.,Wasielewski, E.,Moras, D.,Poterszman, A.,Boelens, R.,Kieffer, B. Solution structure of the C-terminal domain of TFIIH P44 subunit reveals a novel type of C4C4 ring domain involved in protein-protein interactions. J.Biol.Chem., 280:20785-20792, 2005 Cited by PubMed Abstract: The human general transcription factor TFIIH is involved in both transcription and DNA nucleotide excision repair. Among the 10 subunits of the complex, p44 subunit plays a crucial role in both mechanisms. Its N-terminal domain interacts with the XPD helicase, whereas its C-terminal domain is involved specifically in the promoter escape activity. By mutating an exposed and non-conserved cysteine residue into a serine, we produced a soluble mutant of p44-(321-395) suitable for solution structure determination. The domain adopts a C4C4 RING domain structure with sequential organization of beta-strands that is related to canonical RING domains by a circular permutation of the beta-sheet elements. Analysis of the molecular surface and mutagenesis experiments suggests that the binding of p44-(321-395) to TFIIH p34 subunit is not mediated by electrostatic interactions and, thus, differs from previously reported interaction mechanisms involving RING domains. PubMed: 15790571DOI: 10.1074/jbc.M412999200 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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