1exe

<StructureSection load='1exe' size='340' side='right'caption='[[1exe]], [[NMR_Ensembles_of_Models | 23 NMR models]]' scene=''>

<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>

</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>

[[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.

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== 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>

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== References ==

<references/>

[[Category: Bpsp1]]

[[Category: Geiduschek, E P]]

[[Category: Kearns, D R]]

[[Category: Liu, W]]

[[Category: Vu, H M]]

[[Category: Transcription]]