1id0: Difference between revisions

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-{{Seed}}
-[[Image:1id0.png|left|200px]]
-<!--
+==CRYSTAL STRUCTURE OF THE NUCLEOTIDE BOND CONFORMATION OF PHOQ KINASE DOMAIN==
-The line below this paragraph, containing "STRUCTURE_1id0", creates the "Structure Box" on the page.
+<StructureSection load='1id0' size='340' side='right'caption='[[1id0]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1id0]] 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=1ID0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ID0 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-{{STRUCTURE_1id0|  PDB=1id0  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1id0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1id0 OCA], [https://pdbe.org/1id0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1id0 RCSB], [https://www.ebi.ac.uk/pdbsum/1id0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1id0 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PHOQ_ECOLI PHOQ_ECOLI] Member of the two-component regulatory system PhoP/PhoQ involved in adaptation to low Mg(2+) environments and the control of acid resistance genes. In low periplasmic Mg(2+), PhoQ functions as a membrane-associated protein kinase that undergoes autophosphorylation and subsequently transfers the phosphate to PhoP, resulting in the expression of PhoP-activated genes (PAG) and repression of PhoP-repressed genes (PRG). In high periplasmic Mg(2+), acts as a protein phosphatase that dephosphorylates phospho-PhoP, resulting in the repression of PAG and may lead to expression of some PRG (By similarity). PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing (deletion of dsbA/dsbB, or treatment with dithiothreitol). MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway; the 2 periplasmic Cys residues of MgrB are required for its action on PhoQ, which then acts on PhoP. Mediates magnesium influx to the cytosol by activation of mgtA. Promotes expression of the two-component regulatory system rstA/rstB and transcription of the hemL, mgrB, nagA, slyB, vboR and yrbL genes.<ref>PMID:10464230</ref>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/id/1id0_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=1id0 ConSurf].
+<div style="clear:both"></div>
-===CRYSTAL STRUCTURE OF THE NUCLEOTIDE BOND CONFORMATION OF PHOQ KINASE DOMAIN===
+==See Also==
+*[[PhoP-PhoQ|PhoP-PhoQ]]
+== References ==
-<!--
+<references/>
-The line below this paragraph, {{ABSTRACT_PUBMED_11493605}}, adds the Publication Abstract to the page
+__TOC__
-(as it appears on PubMed at http://www.pubmed.gov), where 11493605 is the PubMed ID number.
+</StructureSection>
--->
-{{ABSTRACT_PUBMED_11493605}}
-==About this Structure==
-ID0 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=1ID0 OCA].
-==Reference==
-Structural and mutational analysis of the PhoQ histidine kinase catalytic domain. Insight into the reaction mechanism., Marina A, Mott C, Auyzenberg A, Hendrickson WA, Waldburger CD, J Biol Chem. 2001 Nov 2;276(44):41182-90. Epub 2001 Aug 7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11493605 11493605]
 [[Category: Escherichia coli]]
-[[Category: Non-specific serine/threonine protein kinase]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Auyzenberg A]]
-[[Category: Auyzenberg, A]]
+[[Category: Hendrickson WA]]
-[[Category: Hendrickson, W A.]]
+[[Category: Marina A]]
-[[Category: Marina, A.]]
+[[Category: Mott C]]
-[[Category: Mott, C.]]
+[[Category: Waldburger CD]]
-[[Category: Waldburger, C D.]]
-[[Category: Histidine kinase]]
-[[Category: Phoq/phop]]
-[[Category: Signal transduction]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 10:46:52 2008''