3lis: Difference between revisions

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<StructureSection load='3lis' size='340' side='right'caption='[[3lis]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='3lis' size='340' side='right'caption='[[3lis]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3lis]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Citrobacter_sp._rfl231 Citrobacter sp. rfl231]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LIS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LIS FirstGlance]. <br>
<table><tr><td colspan='2'>[[3lis]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Citrobacter_sp._RFL231 Citrobacter sp. RFL231]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LIS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LIS 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;'>[[3lfp|3lfp]]</div></td></tr>
</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&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">csp231IC ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=315237 Citrobacter sp. RFL231])</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=3lis FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lis OCA], [https://pdbe.org/3lis PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lis RCSB], [https://www.ebi.ac.uk/pdbsum/3lis PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lis 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=3lis FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lis OCA], [https://pdbe.org/3lis PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lis RCSB], [https://www.ebi.ac.uk/pdbsum/3lis PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lis ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/Q32WH4_9ENTR Q32WH4_9ENTR]
Controller proteins play a key role in the temporal regulation of gene expression in bacterial restriction-modification (R-M) systems and are important mediators of horizontal gene transfer. They form the basis of a highly cooperative, concentration-dependent genetic switch involved in both activation and repression of R-M genes. Here we present biophysical, biochemical, and high-resolution structural analyses of a novel class of controller proteins, exemplified by C.Csp231I. In contrast to all previously solved C-protein structures, each protein subunit has two extra helices at the C-terminus, which play a large part in maintaining the dimer interface. The DNA binding site of the protein is also novel, having largely AAAA tracts between the palindromic recognition half-sites, suggesting tight bending of the DNA. The protein structure shows an unusual positively charged surface that could form the basis for wrapping the DNA completely around the C-protein dimer.
 
Structural Analysis of a Novel Class of R-M Controller Proteins: C.Csp231I from Citrobacter sp. RFL231.,McGeehan JE, Streeter SD, Thresh SJ, Taylor JE, Shevtsov MB, Kneale GG J Mol Biol. 2011 Mar 31. PMID:21440553<ref>PMID:21440553</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3lis" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Citrobacter sp. rfl231]]
[[Category: Citrobacter sp. RFL231]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Kneale, G G]]
[[Category: Kneale GG]]
[[Category: McGeehan, J E]]
[[Category: McGeehan JE]]
[[Category: Streeter, S D]]
[[Category: Streeter SD]]
[[Category: Thresh, S J]]
[[Category: Thresh SJ]]
[[Category: Dna binding protein]]
[[Category: Helix-turn-helix]]
[[Category: Restriction modification control]]
[[Category: Transcription]]
[[Category: Transcriptional regulator]]

Latest revision as of 11:46, 7 February 2024

Crystal Structure of the Restriction-Modification Controller Protein C.Csp231I (Monoclinic form)Crystal Structure of the Restriction-Modification Controller Protein C.Csp231I (Monoclinic form)

Structural highlights

3lis is a 2 chain structure with sequence from Citrobacter sp. RFL231. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q32WH4_9ENTR

3lis, resolution 2.00Å

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OCA
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