1rly
From Proteopedia
(New page: 200px<br /> <applet load="1rly" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rly" /> '''RDC-derived models of the zinc ribbon domai...) |
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'''RDC-derived models of the zinc ribbon domain of human general transcription TFIIB (zinc bound structures)'''<br /> | '''RDC-derived models of the zinc ribbon domain of human general transcription TFIIB (zinc bound structures)'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1RLY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1RLY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RLY OCA]. |
==Reference== | ==Reference== | ||
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[[Category: zinc ribbon]] | [[Category: zinc ribbon]] | ||
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Revision as of 14:49, 15 February 2008
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RDC-derived models of the zinc ribbon domain of human general transcription TFIIB (zinc bound 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
1RLY is a Single protein structure of sequence from Homo sapiens with as ligand. 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
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