1mb0: Difference between revisions

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 <StructureSection load='1mb0' size='340' side='right'caption='[[1mb0]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1mb0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cauvi Cauvi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MB0 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1MB0 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1mb0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caulobacter_vibrioides Caulobacter vibrioides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MB0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MB0 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
+</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&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1m5t|1m5t]], [[1mav|1mav]], [[1mb3|1mb3]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">divk ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=155892 CAUVI])</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=1mb0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mb0 OCA], [https://pdbe.org/1mb0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mb0 RCSB], [https://www.ebi.ac.uk/pdbsum/1mb0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mb0 ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1mb0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mb0 OCA], [http://pdbe.org/1mb0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mb0 RCSB], [http://www.ebi.ac.uk/pdbsum/1mb0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mb0 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q9A5I4_CAUVC Q9A5I4_CAUVC]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 19: / Line 20: @@
 </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=1mb0 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-DivK is an essential response regulator in the Gram-negative bacterium Caulobacter crescentus and functions in a complex phosphorelay system that precisely controls the sequence of developmental events during the cell division cycle. Structure determinations of this single domain response regulator at different pH values demonstrated that the five-stranded alpha/beta fold of the DivK protein is fully defined only at acidic pH. The crystal structures of the apoprotein and of metal-bound DivK complexes at higher pH values revealed a synergistic pH- and cation binding-induced flexibility of the beta4-alpha4 loop and of the alpha4 helix. This motion increases the solvent accessibility of the single cysteine residue in the protein. Solution state studies demonstrated a 200-fold pH-dependent increase in the affinity of manganese for the protein between pH 6.0 and 8.5 that seems to involve deprotonation of an acido-basic couple. Taken together, these results suggest that flexibility of critical regions of the protein, ionization of the cysteine 99 residue and improved K(D) values for the catalytic metal ion are coupled events. We propose that the molecular events observed in the isolated protein may be required for DivK activation and that they may be achieved in vivo through the specific protein-protein interactions between the response regulator and its cognate kinases.
-Crystallographic and biochemical studies of DivK reveal novel features of an essential response regulator in Caulobacter crescentus.,Guillet V, Ohta N, Cabantous S, Newton A, Samama JP J Biol Chem. 2002 Nov 1;277(44):42003-10. Epub 2002 Aug 10. PMID:12176983<ref>PMID:12176983</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1mb0" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Response regulator 3D structure|Response regulator 3D structure]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Cauvi]]
+[[Category: Caulobacter vibrioides]]
 [[Category: Large Structures]]
-[[Category: Cabantous, S]]
+[[Category: Cabantous S]]
-[[Category: Guillet, V]]
+[[Category: Guillet V]]
-[[Category: Newton, A]]
+[[Category: Newton A]]
-[[Category: Ohta, N]]
+[[Category: Ohta N]]
-[[Category: SPINE, Structural Proteomics in Europe]]
+[[Category: Samama J-P]]
-[[Category: Samama, J P]]
-[[Category: Cell cycle]]
-[[Category: Response regulator]]
-[[Category: Signal transduction protein]]
-[[Category: Signaling protein]]
-[[Category: Spine]]
-[[Category: Structural genomic]]
-[[Category: Structural proteomics in europe]]