1wrp

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(New page: 200px<br /><applet load="1wrp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wrp, resolution 2.2&Aring;" /> '''FLEXIBILITY OF THE DN...)
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[[Image:1wrp.gif|left|200px]]<br /><applet load="1wrp" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1wrp, resolution 2.2&Aring;" />
 
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'''FLEXIBILITY OF THE DNA-BINDING DOMAINS OF TRP REPRESSOR'''<br />
 
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==Overview==
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==FLEXIBILITY OF THE DNA-BINDING DOMAINS OF TRP REPRESSOR==
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An orthorhombic crystal form of trp repressor (aporepressor plus, L-tryptophan ligand) was solved by molecular replacement, refined to 1.65, A resolution, and compared to the structure of the repressor in trigonal, crystals. Even though these two crystal forms of repressor were grown, under identical conditions, the refined structures have distinctly, different conformations of the DNA-binding domains. Unlike the, repressor/aporepressor structural transition, the conformational shift is, not caused by the binding or loss of the L-tryptophan ligand. We conclude, that while L-tryptophan binding is essential for forming a specific, complex with trp operator DNA, the corepressor ligand does not lock the, repressor into a single conformation that is complementary to the, operator. This flexibility may be required by the various binding modes, proposed for trp repressor in its search for and adherence to its three, different operator sites.
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<StructureSection load='1wrp' size='340' side='right'caption='[[1wrp]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1wrp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WRP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WRP FirstGlance]. <br>
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1WRP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with TRP as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WRP OCA].
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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]] 2.2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</scene></td></tr>
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==Reference==
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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=1wrp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wrp OCA], [https://pdbe.org/1wrp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wrp RCSB], [https://www.ebi.ac.uk/pdbsum/1wrp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wrp ProSAT]</span></td></tr>
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Flexibility of the DNA-binding domains of trp repressor., Lawson CL, Zhang RG, Schevitz RW, Otwinowski Z, Joachimiak A, Sigler PB, Proteins. 1988;3(1):18-31. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=3375234 3375234]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TRPR_ECOLI TRPR_ECOLI] This protein is an aporepressor. When complexed with L-tryptophan it binds the operator region of the trp operon (5'-ACTAGT-'3') and prevents the initiation of transcription. The complex also regulates trp repressor biosynthesis by binding to its regulatory region.
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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/wr/1wrp_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=1wrp ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Joachimiak, A.J.]]
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[[Category: Joachimiak A]]
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[[Category: Lawson, C.L.]]
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[[Category: Lawson CL]]
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[[Category: Otwinowski, Z.]]
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[[Category: Otwinowski Z]]
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[[Category: Schewitz, R.W.]]
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[[Category: Schewitz RW]]
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[[Category: Sigler, P.B.]]
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[[Category: Sigler PB]]
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[[Category: TRP]]
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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 05:37:36 2007''
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Current revision

FLEXIBILITY OF THE DNA-BINDING DOMAINS OF TRP REPRESSOR

PDB ID 1wrp

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