1ro4: Difference between revisions
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<StructureSection load='1ro4' size='340' side='right'caption='[[1ro4]], [[NMR_Ensembles_of_Models | 35 NMR models]]' scene=''> | <StructureSection load='1ro4' size='340' side='right'caption='[[1ro4]], [[NMR_Ensembles_of_Models | 35 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ro4]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1ro4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RO4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RO4 FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1rly|1rly]]</div></td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1rly|1rly]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GTF2B, TFIIB, TF2B ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GTF2B, TFIIB, TF2B ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ro4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ro4 OCA], [https://pdbe.org/1ro4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ro4 RCSB], [https://www.ebi.ac.uk/pdbsum/1ro4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ro4 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/TF2B_HUMAN TF2B_HUMAN]] General factor that plays a major role in the activation of eukaryotic genes transcribed by RNA polymerase II. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 09:31, 2 March 2022
RDC-derived models of the zinc ribbon domain of human general transcription factor TFIIB (zinc free structures)RDC-derived models of the zinc ribbon domain of human general transcription factor TFIIB (zinc free structures)
Structural highlights
Function[TF2B_HUMAN] General factor that plays a major role in the activation of eukaryotic genes transcribed by RNA polymerase II. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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