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3lis

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==Crystal Structure of the Restriction-Modification Controller Protein C.Csp231I (Monoclinic form)==
==Crystal Structure of the Restriction-Modification Controller Protein C.Csp231I (Monoclinic form)==
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<StructureSection load='3lis' size='340' side='right' caption='[[3lis]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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<StructureSection load='3lis' size='340' side='right'caption='[[3lis]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3lis]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LIS FirstGlance]. <br>
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<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>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3lfp|3lfp]]</td></tr>
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</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>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">csp231IC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=315237 Citrobacter sp. RFL231])</td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3lis FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lis OCA], [http://pdbe.org/3lis PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3lis RCSB], [http://www.ebi.ac.uk/pdbsum/3lis PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3lis ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q32WH4_9ENTR Q32WH4_9ENTR]
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3lis" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Citrobacter sp. rfl231]]
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[[Category: Citrobacter sp. RFL231]]
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[[Category: Kneale, G G]]
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[[Category: Large Structures]]
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[[Category: McGeehan, J E]]
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[[Category: Kneale GG]]
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[[Category: Streeter, S D]]
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[[Category: McGeehan JE]]
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[[Category: Thresh, S J]]
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[[Category: Streeter SD]]
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[[Category: Dna binding protein]]
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[[Category: Thresh SJ]]
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[[Category: Helix-turn-helix]]
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[[Category: Restriction modification control]]
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[[Category: Transcription]]
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[[Category: Transcriptional regulator]]
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Current revision

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

PDB ID 3lis

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