2oqr: Difference between revisions

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-[[Image:2oqr.gif|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_2oqr", creates the "Structure Box" on the page.
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-or leave the SCENE parameter empty for the default display.
--->
-{{STRUCTURE_2oqr|  PDB=2oqr  |  SCENE=  }}
-'''The structure of the response regulator RegX3 from Mycobacterium tuberculosis'''
+==The structure of the response regulator RegX3 from Mycobacterium tuberculosis==
+<StructureSection load='2oqr' size='340' side='right'caption='[[2oqr]], [[Resolution|resolution]] 2.03&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2oqr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OQR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OQR FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.03&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=LA:LANTHANUM+(III)+ION'>LA</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2oqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oqr OCA], [https://pdbe.org/2oqr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2oqr RCSB], [https://www.ebi.ac.uk/pdbsum/2oqr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2oqr ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/REGX3_MYCTU REGX3_MYCTU] Probably forms part of a two-component regulatory system regX3/senX3.
+== 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/oq/2oqr_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=2oqr ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The full-length, two-domain response regulator RegX3 from Mycobacterium tuberculosis is a dimer stabilized by three-dimensional domain swapping. Dimerization is known to occur in the OmpR/PhoB subfamily of response regulators upon activation but has previously only been structurally characterized for isolated receiver domains. The RegX3 dimer has a bipartite intermolecular interface, which buries 2357 A(2) per monomer. The two parts of the interface are between the two receiver domains (dimerization interface) and between a composite receiver domain and the effector domain of the second molecule (interdomain interface). The structure provides support for the importance of threonine and tyrosine residues in the signal transduction mechanism. These residues occur in an active-like conformation stabilized by lanthanum ions. In solution, RegX3 exists as both a monomer and a dimer in a concentration-dependent equilibrium. The dimer in solution differs from the active form observed in the crystal, resembling instead the model of the inactive full-length response regulator PhoB.
-==Overview==
+The structure of a full-length response regulator from Mycobacterium tuberculosis in a stabilized three-dimensional domain-swapped, activated state.,King-Scott J, Nowak E, Mylonas E, Panjikar S, Roessle M, Svergun DI, Tucker PA J Biol Chem. 2007 Dec 28;282(52):37717-29. Epub 2007 Oct 16. PMID:17942407<ref>PMID:17942407</ref>
-The full-length, two-domain response regulator RegX3 from Mycobacterium tuberculosis is a dimer stabilized by three-dimensional domain swapping. Dimerization is known to occur in the OmpR/PhoB subfamily of response regulators upon activation but has previously only been structurally characterized for isolated receiver domains. The RegX3 dimer has a bipartite intermolecular interface, which buries 2357 A(2) per monomer. The two parts of the interface are between the two receiver domains (dimerization interface) and between a composite receiver domain and the effector domain of the second molecule (interdomain interface). The structure provides support for the importance of threonine and tyrosine residues in the signal transduction mechanism. These residues occur in an active-like conformation stabilized by lanthanum ions. In solution, RegX3 exists as both a monomer and a dimer in a concentration-dependent equilibrium. The dimer in solution differs from the active form observed in the crystal, resembling instead the model of the inactive full-length response regulator PhoB.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-OQR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OQR OCA].
+</div>
+<div class="pdbe-citations 2oqr" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-The structure of a full-length response regulator from Mycobacterium tuberculosis in a stabilized three-dimensional domain-swapped, activated state., King-Scott J, Nowak E, Mylonas E, Panjikar S, Roessle M, Svergun DI, Tucker PA, J Biol Chem. 2007 Dec 28;282(52):37717-29. Epub 2007 Oct 16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17942407 17942407]
+*[[Response regulator 3D structure|Response regulator 3D structure]]
-[[Category: Mycobacterium tuberculosis]]
+== References ==
-[[Category: Single protein]]
+<references/>
-[[Category: King-Scott, J.]]
+__TOC__
-[[Category: 3d domain swapping]]
+</StructureSection>
-[[Category: Dna-binding]]
+[[Category: Large Structures]]
-[[Category: Regx3]]
+[[Category: Mycobacterium tuberculosis H37Rv]]
-[[Category: Response regulator]]
+[[Category: King-Scott J]]
-[[Category: Transcription,signaling protein]]
-[[Category: Two component system]]
-[[Category: Winged-helix-turn-helix]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 11:28:37 2008''