2JNJ

Solution structure of the p8 TFIIH subunit

Summary for 2JNJ

• Entry DOI: 10.2210/pdb2jnj/pdb
• Descriptor: TFIIH basal transcription factor complex TTD-A subunit (1 entity in total)
• Functional Keywords: protein, transcription, structural genomics, structural proteomics in europe 2, spine-2
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: Q6ZYL4
• Total number of polymer chains: 2
• Total formula weight: 16685.28

Authors

Vitorino, M.,Atkinson, R.A.,Moras, D.,Poterszman, A.,Kieffer, B.,Structural Proteomics in Europe 2 (SPINE-2) (deposition date: 2007-01-26, release date: 2007-04-10, Last modification date: 2023-12-20)

Primary citation

Vitorino, M.,Coin, F.,Zlobinskaya, O.,Atkinson, R.A.,Moras, D.,Egly, J.M.,Poterszman, A.,Kieffer, B.
Solution Structure and Self-association Properties of the p8 TFIIH Subunit Responsible for Trichothiodystrophy
J.Mol.Biol., 368:473-480, 2007

PubMed Abstract: Trichothiodystrophy (TTD) is a rare hereditary multi-system disorder associated with defects in nucleotide excision repair (NER) and transcription as consequences of mutations in XPB, XPD and p8/TTD-A subunits of transcription factor IIH (TFIIH). Here, we report the solution structure of the p8/TTD-A protein, a small alpha/beta protein built around an antiparallel beta-sheet that forms a homodimer with an extended interface. In order to characterize the dimer interface, we have introduced a mutation at position 44, which destabilizes the dimeric form of the protein. We have shown that this mutation has no effect on the intrinsic ability of p8/TTD-A to stimulate NER in vitro, but affects the capacity of p8/TTD-A to restore TFIIH concentration in TTD-A fibroblasts. Point mutations found in TTD-A patients are discussed on the basis of the present structure.

PubMed: 17350038
DOI: 10.1016/j.jmb.2007.02.020

Experimental method

SOLUTION NMR