6fxa
From Proteopedia
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(New page: '''Unreleased structure''' The entry 6fxa is ON HOLD Authors: Description: Category: Unreleased Structures) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Dimerization domain of TP901-1 CI repressor== | |
| + | <StructureSection load='6fxa' size='340' side='right'caption='[[6fxa]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6fxa]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactococcus_phage_TP901-1 Lactococcus phage TP901-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FXA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6FXA FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=6fxa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fxa OCA], [https://pdbe.org/6fxa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6fxa RCSB], [https://www.ebi.ac.uk/pdbsum/6fxa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6fxa ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/O48503_9CAUD O48503_9CAUD] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Temperate bacteriophages are known for their bistability, which in TP901-1 is controlled by two proteins, CI and MOR. Clear 1 repressor (CI) is hexameric and binds three palindromic operator sites via an N-terminal helix-turn-helix domain (NTD). A dimeric form, such as the truncated CI58 investigated here, is necessary for high-affinity binding to DNA. The crystal structure of the dimerization region (CTD1 ) is determined here, showing that it forms a pair of helical hooks. This newly determined structure is used together with the known crystal structure of the CI-NTD and small angle X-ray scattering data, to determine the solution structure of CI58 in complex with a palindromic operator site, showing that the two NTDs bind on opposing sides of the DNA helix. | ||
| - | + | Structural basis of the bacteriophage TP901-1 CI repressor dimerization and interaction with DNA.,Rasmussen KK, Varming AK, Schmidt SN, Frandsen KEH, Thulstrup PW, Jensen MR, Lo Leggio L FEBS Lett. 2018 Apr 23. doi: 10.1002/1873-3468.13060. PMID:29683476<ref>PMID:29683476</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6fxa" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Lactococcus phage TP901-1]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Lo Leggio L]] | ||
| + | [[Category: Rasmussen KK]] | ||
| + | [[Category: Varming AK]] | ||
Current revision
Dimerization domain of TP901-1 CI repressor
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