1F3U

CRYSTAL STRUCTURE OF THE RAP30/74 INTERACTION DOMAINS OF HUMAN TFIIF

Summary for 1F3U

• Entry DOI: 10.2210/pdb1f3u/pdb
• Descriptor: TRANSCRIPTION INITIATION FACTOR IIF, BETA SUBUNIT, TRANSCRIPTION INITIATION FACTOR IIF, ALPHA SUBUNIT (3 entities in total)
• Functional Keywords: general transcription initiation and elongation factor, rna polymerase ii, novel dimerization fold, beta barrel, transcription
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: P13984 P35269
• Total number of polymer chains: 8
• Total formula weight: 130643.12

Authors

Gaiser, F.,Tan, S.,Richmond, T.J. (deposition date: 2000-06-06, release date: 2000-10-11, Last modification date: 2024-02-07)

Primary citation

Gaiser, F.,Tan, S.,Richmond, T.J.
Novel dimerization fold of RAP30/RAP74 in human TFIIF at 1.7 A resolution.
J.Mol.Biol., 302:1119-1127, 2000

PubMed Abstract: General transcription factor IIF (TFIIF) is required for transcription by RNA polymerase II; it consists minimally of a heterodimer of RNA polymerase-associated proteins RAP30 and RAP74. According to solution and mutagenesis studies, the multiple domains of RAP30 and RAP74 bind PolII, TFIIB, TAF250 and DNA in interactions that are essential for transcription initiation and elongation. The X-ray structure of the RAP30/RAP74 interaction domains at 1.7 A resolution reveals a novel "triple barrel" dimerization fold and suggests with mutant data that interactions with the transcription apparatus are mediated not only by this tripartite beta-barrel, but also via flexible loops and alpha and beta-structures extending from it.

PubMed: 11183778
DOI: 10.1006/jmbi.2000.4110

Experimental method

X-RAY DIFFRACTION (1.7 Å)