4iwr: Difference between revisions
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==C.Esp1396I bound to a 25 base pair operator site== | ==C.Esp1396I bound to a 25 base pair operator site== | ||
<StructureSection load='4iwr' size='340' side='right' caption='[[4iwr]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='4iwr' size='340' side='right'caption='[[4iwr]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4iwr]] is a 8 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4iwr]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterobacter_sp._RFL1396 Enterobacter sp. RFL1396]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IWR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IWR FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</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=4iwr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4iwr OCA], [https://pdbe.org/4iwr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4iwr RCSB], [https://www.ebi.ac.uk/pdbsum/4iwr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4iwr ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q8GGH0_9ENTR Q8GGH0_9ENTR] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4iwr" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Enterobacter sp. | [[Category: Enterobacter sp. RFL1396]] | ||
[[Category: Ball | [[Category: Large Structures]] | ||
[[Category: Kneale | [[Category: Ball NJ]] | ||
[[Category: Martin | [[Category: Kneale GG]] | ||
[[Category: McGeehan | [[Category: Martin RNA]] | ||
[[Category: Streeter | [[Category: McGeehan JE]] | ||
[[Category: Thresh | [[Category: Streeter SD]] | ||
[[Category: Thresh S-J]] | |||
Latest revision as of 18:32, 20 September 2023
C.Esp1396I bound to a 25 base pair operator siteC.Esp1396I bound to a 25 base pair operator site
Structural highlights
FunctionPublication Abstract from PubMedThe controller protein of the type II restriction-modification (RM) system Esp1396I binds to three distinct DNA operator sequences upstream of the methyltransferase and endonuclease genes in order to regulate their expression. Previous biophysical and crystallographic studies have shown molecular details of how the controller protein binds to the operator sites with very different affinities. Here, two protein-DNA co-crystal structures containing portions of unbound DNA from native operator sites are reported. The DNA in both complexes shows significant distortion in the region between the conserved symmetric sequences, similar to that of a DNA duplex when bound by the controller protein (C-protein), indicating that the naked DNA has an intrinsic tendency to bend when not bound to the C-protein. Moreover, the width of the major groove of the DNA adjacent to a bound C-protein dimer is observed to be significantly increased, supporting the idea that this DNA distortion contributes to the substantial cooperativity found when a second C-protein dimer binds to the operator to form the tetrameric repression complex. Structural analysis of DNA-protein complexes regulating the restriction-modification system Esp1396I.,Martin RN, McGeehan JE, Ball NJ, Streeter SD, Thresh SJ, Kneale GG Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Sep;69(Pt 9):962-6. doi:, 10.1107/S174430911302126X. Epub 2013 Aug 19. PMID:23989141[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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