2pub

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(New page: 200px<br /><applet load="2pub" size="450" color="white" frame="true" align="right" spinBox="true" caption="2pub, resolution 2.700&Aring;" /> '''CRYSTAL STRUCTURE O...)
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[[Image:2pub.gif|left|200px]]<br /><applet load="2pub" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2pub, resolution 2.700&Aring;" />
 
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'''CRYSTAL STRUCTURE OF THE LACI FAMILY MEMBER, PURR, BOUND TO DNA: MINOR GROOVE BINDING BY ALPHA HELICES'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF THE LACI FAMILY MEMBER, PURR, BOUND TO DNA: MINOR GROOVE BINDING BY ALPHA HELICES==
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The three-dimensional structure of a ternary complex of the purine, repressor, PurR, bound to both its corepressor, hypoxanthine, and the, 16-base pair purF operator site has been solved at 2.7 A resolution by, x-ray crystallography. The bipartite structure of PurR consists of an, amino-terminal DNA-binding domain and a larger carboxyl-terminal, corepressor binding and dimerization domain that is similar to that of the, bacterial periplasmic binding proteins. The DNA-binding domain contains a, helix-turn-helix motif that makes base-specific contacts in the major, groove of the DNA. Base contacts are also made by residues of, symmetry-related alpha helices, the "hinge" helices, which bind deeply in, the minor groove. Critical to hinge helix-minor groove binding is the, intercalation of the side chains of Leu54 and its symmetry-related mate, Leu54', into the central CpG-base pair step. These residues thereby act as, "leucine levers" to pry open the minor groove and kink the purF operator, by 45 degrees.
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<StructureSection load='2pub' size='340' side='right'caption='[[2pub]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2pub]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PUB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PUB 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]] 2.7&#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=ADE:ADENINE'>ADE</scene></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=2pub FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pub OCA], [https://pdbe.org/2pub PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pub RCSB], [https://www.ebi.ac.uk/pdbsum/2pub PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pub ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PURR_ECOLI PURR_ECOLI] Is the main repressor of the genes involved in the de novo synthesis of purine nucleotides, regulating purB, purC, purEK, purF, purHD, purL, purMN and guaBA expression. In addition, it participates in the regulation or coregulation of genes involved in de novo pyrimidine nucleotide biosynthesis, salvage and uptake (pyrC, pyrD, carAB and codBA), and of several genes encoding enzymes necessary for nucleotide and polyamine biosynthesis (prsA, glyA, gcvTHP, speA, glnB). Binds to a 16-bp palindromic sequence located within the promoter region of pur regulon genes. The consensus binding sequence is 5'-ACGCAAACGTTTTCNT-3'. PurR is allosterically activated to bind its cognate DNA by binding the purine corepressors, hypoxanthine or guanine, thereby effecting transcription repression.<ref>PMID:2404765</ref> <ref>PMID:2211500</ref> <ref>PMID:1400170</ref> <ref>PMID:14741201</ref>
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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/pu/2pub_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=2pub 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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2PUB 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 ADE as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2PUB OCA].
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*[[Purine repressor|Purine repressor]]
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== References ==
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==Reference==
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<references/>
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Crystal structure of LacI member, PurR, bound to DNA: minor groove binding by alpha helices., Schumacher MA, Choi KY, Zalkin H, Brennan RG, Science. 1994 Nov 4;266(5186):763-70. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7973627 7973627]
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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: Choi, K.Y.]]
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[[Category: Synthetic construct]]
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[[Category: Schumacher, R.G.Brennan M.A.]]
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[[Category: Brennan MA]]
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[[Category: Zalkin, H.]]
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[[Category: Choi KY]]
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[[Category: ADE]]
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[[Category: Schumacher RG]]
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[[Category: complex (dna-binding protein/dna)]]
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[[Category: Zalkin H]]
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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 13:40:25 2007''
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Current revision

CRYSTAL STRUCTURE OF THE LACI FAMILY MEMBER, PURR, BOUND TO DNA: MINOR GROOVE BINDING BY ALPHA HELICES

PDB ID 2pub

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