2f23

<StructureSection load='2f23' size='340' side='right' caption='[[2f23]], [[Resolution|resolution]] 1.60&Aring;' scene=''>

<table><tr><td colspan='2'>[[2f23]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thet2 Thet2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F23 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2F23 FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gfh1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=262724 THET2])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2f23 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f23 OCA], [http://pdbe.org/2f23 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2f23 RCSB], [http://www.ebi.ac.uk/pdbsum/2f23 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2f23 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/GFH1_THET2 GFH1_THET2]] Inhibits all catalytic activities of RNA polymerase (RNAP) by partially occluding its substrate-binding site and preventing NTP binding.<ref>PMID:16628221</ref>

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== Publication Abstract from PubMed ==

Gfh1, a transcription factor from Thermus thermophilus, inhibits all catalytic activities of RNA polymerase (RNAP). We characterized the Gfh1 structure, function and possible mechanism of action and regulation. Gfh1 inhibits RNAP by competing with NTPs for coordinating the active site Mg2+ ion. This coordination requires at least two aspartates at the tip of the Gfh1 N-terminal coiled-coil domain (NTD). The overall structure of Gfh1 is similar to that of the Escherichia coli transcript cleavage factor GreA, except for the flipped orientation of the C-terminal domain (CTD). We show that depending on pH, Gfh1-CTD exists in two alternative orientations. At pH above 7, it assumes an inactive 'flipped' orientation seen in the structure, which prevents Gfh1 from binding to RNAP. At lower pH, Gfh1-CTD switches to an active 'Gre-like' orientation, which enables Gfh1 to bind to and inhibit RNAP.

pH-dependent conformational switch activates the inhibitor of transcription elongation.,Laptenko O, Kim SS, Lee J, Starodubtseva M, Cava F, Berenguer J, Kong XP, Borukhov S EMBO J. 2006 May 17;25(10):2131-41. Epub 2006 Apr 20. PMID:16628221<ref>PMID:16628221</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 2f23" style="background-color:#fffaf0;"></div>

[[Category: Thet2]]

[[Category: Kim, S S]]

[[Category: Kong, X P]]

[[Category: Crystal structure anti-grea gfh1 thermus thermophilus]]

[[Category: Transcription]]