3lfp: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==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 20:12, 18 December 2014
Crystal Structure of the Restriction-Modification Controller Protein C.Csp231ICrystal Structure of the Restriction-Modification Controller Protein C.Csp231I
Structural highlights
Publication Abstract from PubMedController 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||