1zes: Difference between revisions

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-[[Image:1zes.gif|left|200px]]
- {{Structure
+==BeF3- activated PhoB receiver domain==
-|PDB= 1zes |SIZE=350|CAPTION= <scene name='initialview01'>1zes</scene>, resolution 1.90&Aring;
+<StructureSection load='1zes' size='340' side='right'caption='[[1zes]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
+<table><tr><td colspan='2'>[[1zes]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. The October 2015 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Two-component Systems''  by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2015_10 10.2210/rcsb_pdb/mom_2015_10]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZES OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZES FirstGlance]. <br>
-|ACTIVITY=
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
-|GENE= phoB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-|DOMAIN=
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zes FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zes OCA], [https://pdbe.org/1zes PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zes RCSB], [https://www.ebi.ac.uk/pdbsum/1zes PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zes ProSAT]</span></td></tr>
-|RELATEDENTRY=
+</table>
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zes FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zes OCA], [http://www.ebi.ac.uk/pdbsum/1zes PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zes RCSB]</span>
+== Function ==
-}}
+[https://www.uniprot.org/uniprot/PHOB_ECOLI PHOB_ECOLI] This protein is a positive regulator for the phosphate regulon. Transcription of this operon is positively regulated by PhoB and PhoR when phosphate is limited.
+== Evolutionary Conservation ==
-'''BeF3- activated PhoB receiver domain'''
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
-==Overview==
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ze/1zes_consurf.spt"</scriptWhenChecked>
-Response regulators (RRs), which undergo phosphorylation/dephosphorylation at aspartate residues, are highly prevalent in bacterial signal transduction. RRs typically contain an N-terminal receiver domain that regulates the activities of a C-terminal DNA binding domain in a phosphorylation-dependent manner. We present crystallography and solution NMR data for the receiver domain of Escherichia coli PhoB which show distinct 2-fold symmetric dimers in the inactive and active states. These structures, together with the previously determined structure of the C-terminal domain of PhoB bound to DNA, define the conformation of the active transcription factor and provide a model for the mechanism of activation in the OmpR/PhoB subfamily, the largest group of RRs. In the active state, the receiver domains dimerize with 2-fold rotational symmetry using their alpha4-beta5-alpha5 faces, while the effector domains bind to DNA direct repeats with tandem symmetry, implying a loss of intramolecular interactions.
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
-==About this Structure==
+  </jmolCheckbox>
-ZES is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZES OCA].
+</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=1zes ConSurf].
+<div style="clear:both"></div>
-==Reference==
+__TOC__
-Mechanism of activation for transcription factor PhoB suggested by different modes of dimerization in the inactive and active states., Bachhawat P, Swapna GV, Montelione GT, Stock AM, Structure. 2005 Sep;13(9):1353-63. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16154092 16154092]
+</StructureSection>
 [[Category: Escherichia coli]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Bachhawat, P.]]
+[[Category: RCSB PDB Molecule of the Month]]
-[[Category: Montelione, G T.]]
+[[Category: Two-component Systems]]
-[[Category: Stock, A M.]]
+[[Category: Bachhawat P]]
-[[Category: activated]]
+[[Category: Montelione GT]]
-[[Category: chey-like fold]]
+[[Category: Stock AM]]
-[[Category: phob]]
-[[Category: response regulator]]
-[[Category: transcription factor]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:34:57 2008''