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==SOLUTION STRUCTURE OF A MUTANT OF TRANSCRIPTION FACTOR 1.==
==SOLUTION STRUCTURE OF A MUTANT OF TRANSCRIPTION FACTOR 1.==
<StructureSection load='1exe' size='340' side='right'caption='[[1exe]], [[NMR_Ensembles_of_Models | 23 NMR models]]' scene=''>
<StructureSection load='1exe' size='340' side='right'caption='[[1exe]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1exe]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bpsp1 Bpsp1]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EXE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EXE FirstGlance]. <br>
<table><tr><td colspan='2'>[[1exe]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_virus_SPO1 Bacillus virus SPO1]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EXE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EXE 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;'>[[1wtu|1wtu]]</div></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1exe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1exe OCA], [https://pdbe.org/1exe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1exe RCSB], [https://www.ebi.ac.uk/pdbsum/1exe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1exe ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1exe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1exe OCA], [https://pdbe.org/1exe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1exe RCSB], [https://www.ebi.ac.uk/pdbsum/1exe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1exe ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/TF1_BPSP1 TF1_BPSP1]] Selectively binds to and inhibits the transcription of hydroxymethyluracil-(hmUra)-containing DNA, such as SP01 DNA, by RNA polymerase in vitro.  
[https://www.uniprot.org/uniprot/TF1_BPSP1 TF1_BPSP1] Selectively binds to and inhibits the transcription of hydroxymethyluracil-(hmUra)-containing DNA, such as SP01 DNA, by RNA polymerase in vitro.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1exe ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1exe ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
An NMR solution structure of a mutant of the homodimer protein transcription factor 1, TF1-G15/I32 (22 kDa), has been solved to atomic resolution, with 23 final structures that converge to an r.m. s.d. of 0.78 A. The overall shape of TF1-G15/I32 remains similar to that of the wild-type protein and other type II DNA-binding proteins. Each monomer has two N-terminal alpha-helices separated by a short loop, followed by a three-stranded beta-sheet, whose extension between the second and third beta-strands forms an antiparallel beta-ribbon arm, leading to a C-terminal third alpha-helix that is severely kinked in the middle. Close examination of the structure of TF1-G15/I32 reveals why it is more stable and binds DNA more tightly than does its wild-type counterpart. The dimeric core, consisting of the N-terminal helices and the beta-sheets, is more tightly packed, and this might be responsible for its increased thermal stability. The DNA-binding domain, composed of the top face of the beta-sheet, the beta-ribbon arms and the C-terminal helices, is little changed from wild-type TF1. Rather, the enhancement in DNA affinity must be due almost exclusively to the creation of an additional DNA-binding site at the side of the dimer by changes affecting helices 1 and 2: helix 2 of TF1-G15/I32 is one residue longer than helix 2 of the wild-type protein, bends inward, and is both translationally and rotationally displaced relative to helix 1. This rearrangement creates a longer, narrower fissure between the V-shaped N-terminal helices and exposes additional positively charged surface at each side of the dimer.
Solution structure of a mutant of transcription factor 1: implications for enhanced DNA binding.,Liu W, Vu HM, Geiduschek EP, Kearns DR J Mol Biol. 2000 Sep 29;302(4):821-30. PMID:10993726<ref>PMID:10993726</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1exe" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bpsp1]]
[[Category: Bacillus virus SPO1]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Geiduschek, E P]]
[[Category: Geiduschek EP]]
[[Category: Kearns, D R]]
[[Category: Kearns DR]]
[[Category: Liu, W]]
[[Category: Liu W]]
[[Category: Vu, H M]]
[[Category: Vu HM]]
[[Category: Beta ribbon arm]]
[[Category: Dna-bending protein]]
[[Category: Dna-binding]]
[[Category: Transcription]]
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