1ro4
From Proteopedia
|
RDC-derived models of the zinc ribbon domain of human general transcription factor TFIIB (zinc free structures)
Overview
The general transcription factor, TFIIB, plays an important role in the, assembly of the pre-initiation complex. The N-terminal domain (NTD) of, TFIIB contains a zinc-ribbon motif, which is responsible for the, recruitment of RNA polymerase II and TFIIF to the core promoter region., Although zinc-ribbon motif structures of eukaryotic and archaeal TFIIBs, have been reported previously, the structural role of Zn2 binding to TFIIB, remains to be determined. In the present paper, we report NMR and, biochemical studies of human TFIIB NTD, which characterize the structure, and dynamics of the TFIIB Zn2-binding domain in both Zn2-bound and -free, states. The NMR data show that, whereas the backbone fold of NTD is, pre-formed in the apo state, Zn2 binding reduces backbone mobility in the, b-turn (Arg28-Gly30), induces enhanced structural rigidity of the, charged-cluster domain in the central linker region of TFIIB and appends a, positive surface charge within the Zn2-binding site. V8, protease-sensitivity assays of full-length TFIIB support the Zn2-dependent, structural changes. These structural effects of Zn2 binding on TFIIB may, have a critical role in interactions with its binding partners, such as, the Rpb1 subunit of RNA polymerase II.
About this Structure
1RO4 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Probing Zn2+-binding effects on the zinc-ribbon domain of human general transcription factor TFIIB., Ghosh M, Elsby LM, Mal TK, Gooding JM, Roberts SG, Ikura M, Biochem J. 2004 Mar 1;378(Pt 2):317-24. PMID:14641108
Page seeded by OCA on Mon Nov 12 19:05:49 2007
