4pn7

Crystal Structure of the TFIIH p34 N-terminal Domain

spinqualitylabelsall models 4pn7, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4pn7 is a 1 chain structure with sequence from Chaetomium thermophilum var. thermophilum DSM 1495. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.801Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function G0RXV8_CHATD Publication Abstract from PubMed RNA polymerase II dependent transcription and nucleotide excision repair are mediated by a multifaceted interplay of subunits within the general transcription factor II H (TFIIH). A better understanding of the molecular structure of TFIIH is the key to unravel the mechanism of action of this versatile protein complex within these vital cellular processes. The importance of this complex becomes further evident in the context of severe diseases like xeroderma pigmentosum, Cockayne's syndrome and trichothiodystrophy, that arise from single point mutations in TFIIH subunits. Here we describe the structure of the p34 subunit of the TFIIH complex from the eukaryotic thermophilic fungus Chaetomium thermophilum. The structure revealed that p34 contains a von Willebrand Factor A (vWA) like domain, a fold which is generally known to be involved in protein-protein interactions. Within TFIIH p34 strongly interacts with p44, a positive regulator of the helicase XPD. Putative protein-protein interfaces are analyzed and possible binding sites for the p34-p44 interaction suggested. The Structure of the TFIIH p34 Subunit Reveals a Von Willebrand Factor A Like Fold.,Schmitt DR, Kuper J, Elias A, Kisker C PLoS One. 2014 Jul 11;9(7):e102389. doi: 10.1371/journal.pone.0102389., eCollection 2014. PMID:25013903 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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