1PFJ

Solution structure of the N-terminal PH/PTB domain of the TFIIH P62 subunit

Summary for 1PFJ

• Entry DOI: 10.2210/pdb1pfj/pdb
• Descriptor: TFIIH basal transcription factor complex p62 subunit (1 entity in total)
• Functional Keywords: ph/ptb domain, structural proteomics in europe, spine, structural genomics, transcription
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: P32780
• Total number of polymer chains: 1
• Total formula weight: 12306.32

Authors

Gervais, V.,Lamour, V.,Jawhari, A.,Frindel, F.,Wasielewski, E.,Thierry, J.C.,Kieffer, B.,Poterszman, A.,Structural Proteomics in Europe (SPINE) (deposition date: 2003-05-27, release date: 2004-06-08, Last modification date: 2024-05-22)

Primary citation

Gervais, V.,Lamour, V.,Jawhari, A.,Frindel, F.,Wasielewski, E.,Dubaele, S.,Egly, J.M.,Thierry, J.C.,Kieffer, B.,Poterszman, A.
TFIIH contains a PH domain involved in DNA nucleotide excision repair.
Nat.Struct.Mol.Biol., 11:616-622, 2004

PubMed Abstract: The human general transcription factor TFIIH is involved in both transcription and DNA repair. We have identified a structural domain in the core subunit of TFIIH, p62, which is absolutely required for DNA repair activity through the nucleotide excision repair pathway. Using coimmunoprecipitation experiments, we showed that this activity involves the interaction between the N-terminal domain of p62 and the 3' endonuclease XPG, a major component of the nucleotide excision repair machinery. Furthermore, we reconstituted a functional TFIIH particle with a mutant of p62 lacking the N-terminal domain, showing that this domain is not required for assembly of the TFIIH complex and basal transcription. We solved its three-dimensional structure and found an unpredicted pleckstrin homology and phosphotyrosine binding (PH/PTB) domain, uncovering a new class of activity for this fold.

PubMed: 15195146
DOI: 10.1038/nsmb782

Experimental method

SOLUTION NMR