1xxc: Difference between revisions

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 <StructureSection load='1xxc' size='340' side='right'caption='[[1xxc]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1xxc]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XXC OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1XXC FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1xxc]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XXC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XXC FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">T7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1xxc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xxc OCA], [http://pdbe.org/1xxc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xxc RCSB], [http://www.ebi.ac.uk/pdbsum/1xxc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1xxc ProSAT]</span></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=1xxc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xxc OCA], [https://pdbe.org/1xxc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xxc RCSB], [https://www.ebi.ac.uk/pdbsum/1xxc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xxc ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/ARGR_ECOLI ARGR_ECOLI]] Negatively controls the expression of the four operons of arginine biosynthesis in addition to the carAB operon. Predominantly interacts with A/T residues in ARG boxes. It also binds to a specific site in cer locus. Thus it is essential for cer-mediated site-specific recombination in ColE1. It is necessary for monomerization of the plasmid ColE1.
+[https://www.uniprot.org/uniprot/ARGR_ECOLI ARGR_ECOLI] Negatively controls the expression of the four operons of arginine biosynthesis in addition to the carAB operon. Predominantly interacts with A/T residues in ARG boxes. It also binds to a specific site in cer locus. Thus it is essential for cer-mediated site-specific recombination in ColE1. It is necessary for monomerization of the plasmid ColE1.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1xxc ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The structure of the oligomerization and L-arginine binding domain of the Escherichia coli arginine repressor (ArgR) has been determined using X-ray diffraction methods at 2.2 A resolution with bound arginine and at 2.8 A in the unliganded form. The oligomeric core is a 3-fold rotationally symmetric hexamer formed from six identical subunits corresponding to the 77 C-terminal residues (80 to 156) of ArgR. Each subunit has an alpha/beta fold containing a four-stranded antiparallel beta-sheet and two antiparallel alpha-helices. The hexamer is formed from two trimers, each with tightly packed hydrophobic cores. In the absence of arginine, the trimers stack back-to-back through a dyad-symmetric, sparsely packed hydrophobic interface. Six molecules of arginine bind at the trimer-trimer interface, each making ten hydrogen bonds to the protein including a direct ion pair that crosslinks the two protein trimers. Solution experiments with wild-type ArgR and oligomerization domain indicate that the hexameric form is greatly stabilized upon arginine binding. The crystal structures and solution experiments together suggest possible mechanisms of how arginine activates ArgR to bind to its DNA targets and provides a stereochemical basis for interpreting the results of mutagenesis and biochemical experiments with ArgR.
-Structure of the oligomerization and L-arginine binding domain of the arginine repressor of Escherichia coli.,Van Duyne GD, Ghosh G, Maas WK, Sigler PB J Mol Biol. 1996 Feb 23;256(2):377-91. PMID:8594204<ref>PMID:8594204</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1xxc" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Arginine repressor 3D structures|Arginine repressor 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Ecoli]]
+[[Category: Escherichia coli K-12]]
 [[Category: Large Structures]]
-[[Category: Duyne, G D.Van]]
+[[Category: Ghosh G]]
-[[Category: Ghosh, G]]
+[[Category: Maas WK]]
-[[Category: Maas, W K]]
+[[Category: Sigler PB]]
-[[Category: Sigler, P B]]
+[[Category: Van Duyne GD]]
-[[Category: Dna binding regulatory protein]]