1BH9

HTAFII18/HTAFII28 HETERODIMER CRYSTAL STRUCTURE WITH BOUND PCMBS

Summary for 1BH9

• Entry DOI: 10.2210/pdb1bh9/pdb
• Descriptor: TAFII18, TAFII28, PARA-MERCURY-BENZENESULFONIC ACID, ... (4 entities in total)
• Functional Keywords: htafii18, histone fold, tata binding protein, transcription regulation complex
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus : Q15543 Q15544
• Total number of polymer chains: 2
• Total formula weight: 15745.57

Authors

Birck, C.,Poch, O.,Romier, C.,Ruff, M.,Mengus, G.,Lavigne, A.-C.,Davidson, I.,Moras, D. (deposition date: 1998-06-16, release date: 1999-06-22, Last modification date: 2024-02-07)

Primary citation

Birck, C.,Poch, O.,Romier, C.,Ruff, M.,Mengus, G.,Lavigne, A.C.,Davidson, I.,Moras, D.
Human TAF(II)28 and TAF(II)18 interact through a histone fold encoded by atypical evolutionary conserved motifs also found in the SPT3 family.
Cell(Cambridge,Mass.), 94:239-249, 1998

PubMed Abstract: Determination of the crystal structure of the human TBP-associated factor (hTAF(II))28/hTAF(II)18 heterodimer shows that these TAF(II)s form a novel histone-like pair in the TFIID complex. The histone folds in hTAF(II)28 and hTAF(II)18 were not predicted from their primary sequence, indicating that these TAF(II)s define a novel family of atypical histone fold sequences. The TAF(II)18 and TAF(II)28 histone fold motifs are also present in the N- and C-terminal regions of the SPT3 proteins, suggesting that the histone fold in SPT3 may be reconstituted by intramolecular rather than classical intermolecular interactions. The existence of additional histone-like pairs in both the TFIID and SAGA complexes shows that the histone fold is a more commonly used motif for mediating TAF-TAF interactions than previously believed.

PubMed: 9695952
DOI: 10.1016/S0092-8674(00)81423-3

Experimental method

X-RAY DIFFRACTION (2.6 Å)