3lfp: 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 [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=3LFP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LFP FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</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=3lfp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lfp OCA], [https://pdbe.org/3lfp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lfp RCSB], [https://www.ebi.ac.uk/pdbsum/3lfp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lfp ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q32WH4_9ENTR Q32WH4_9ENTR] | |||
<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> | ||
[[ | <div class="pdbe-citations 3lfp" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: Kneale | <references/> | ||
[[Category: McGeehan | __TOC__ | ||
[[Category: Streeter | </StructureSection> | ||
[[Category: Thresh | [[Category: Citrobacter sp. RFL231]] | ||
[[Category: Large Structures]] | |||
[[Category: Kneale GG]] | |||
[[Category: McGeehan JE]] | |||
[[Category: Streeter SD]] | |||
[[Category: Thresh SJ]] | |||
Latest revision as of 11:36, 6 September 2023
Crystal Structure of the Restriction-Modification Controller Protein C.Csp231ICrystal Structure of the Restriction-Modification Controller Protein C.Csp231I
Structural highlights
FunctionPublication 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
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