3lfp: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 3lfp is ON HOLD  until Paper Publication
+==Crystal Structure of the Restriction-Modification Controller Protein C.Csp231I==
+<StructureSection load='3lfp' size='340' side='right'caption='[[3lfp]], [[Resolution|resolution]] 2.00&Aring;' 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]] 2&#8491;</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.
-Authors: McGeehan, J.E., Streeter, S.D., Thresh, S.J., Kneale, G.G.
+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>
-Description: Crystal Structure of the Restriction-Modification Controller Protein C.Csp231I
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr  7 10:19:45 2010''
+<div class="pdbe-citations 3lfp" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Citrobacter sp. RFL231]]
+[[Category: Large Structures]]
+[[Category: Kneale GG]]
+[[Category: McGeehan JE]]
+[[Category: Streeter SD]]
+[[Category: Thresh SJ]]