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3lfp
From Proteopedia
(Difference between revisions)
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| - | + | ==Crystal Structure of the Restriction-Modification Controller Protein C.Csp231I== | |
| - | + | <StructureSection load='3lfp' size='340' side='right' caption='[[3lfp]], [[Resolution|resolution]] 2.00Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[3lfp]] is a 1 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=3LFP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LFP FirstGlance]. <br> | ||
| + | </td></tr><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> | ||
| + | <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=3lfp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lfp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lfp RCSB], [http://www.ebi.ac.uk/pdbsum/3lfp PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Citrobacter sp. rfl231]] | [[Category: Citrobacter sp. rfl231]] | ||
| - | [[Category: Kneale, G G | + | [[Category: Kneale, G G]] |
| - | [[Category: McGeehan, J E | + | [[Category: McGeehan, J E]] |
| - | [[Category: Streeter, S D | + | [[Category: Streeter, S D]] |
| - | [[Category: Thresh, S J | + | [[Category: Thresh, S J]] |
[[Category: Dna binding protein]] | [[Category: Dna binding protein]] | ||
[[Category: Helix-turn-helix]] | [[Category: Helix-turn-helix]] | ||
Revision as of 17:12, 18 December 2014
Crystal Structure of the Restriction-Modification Controller Protein C.Csp231I
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