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1xxc

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(New page: 200px<br /><applet load="1xxc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xxc, resolution 2.8&Aring;" /> '''C-TERMINAL DOMAIN OF ...)
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[[Image:1xxc.jpg|left|200px]]<br /><applet load="1xxc" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1xxc, resolution 2.8&Aring;" />
 
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'''C-TERMINAL DOMAIN OF ESCHERICHIA COLI ARGININE REPRESSOR'''<br />
 
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==Overview==
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==C-TERMINAL DOMAIN OF ESCHERICHIA COLI ARGININE REPRESSOR==
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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.
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<StructureSection load='1xxc' size='340' side='right'caption='[[1xxc]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</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>
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<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>
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xx/1xxc_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1XXC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XXC OCA].
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*[[Arginine repressor 3D structures|Arginine repressor 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8594204 8594204]
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[[Category: Escherichia coli K-12]]
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[[Category: Escherichia coli]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Ghosh G]]
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[[Category: Duyne, G.D.Van.]]
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[[Category: Maas WK]]
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[[Category: Ghosh, G.]]
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[[Category: Sigler PB]]
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[[Category: Maas, W.K.]]
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[[Category: Van Duyne GD]]
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[[Category: Sigler, P.B.]]
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[[Category: dna binding regulatory protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:24:39 2007''
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Current revision

C-TERMINAL DOMAIN OF ESCHERICHIA COLI ARGININE REPRESSOR

PDB ID 1xxc

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