1mb0: Difference between revisions
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==CRYSTAL STRUCTURE OF THE RESPONSE REGULATOR DIVK AT PH 8.0 IN COMPLEX WITH MN2+== | ==CRYSTAL STRUCTURE OF THE RESPONSE REGULATOR DIVK AT PH 8.0 IN COMPLEX WITH MN2+== | ||
<StructureSection load='1mb0' size='340' side='right' caption='[[1mb0]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1mb0' size='340' side='right'caption='[[1mb0]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == 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:// | <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> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr> | </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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1m5t|1m5t]], [[1mav|1mav]], [[1mb3|1mb3]]</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='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='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'>[http:// | <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> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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</div> | </div> | ||
<div class="pdbe-citations 1mb0" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1mb0" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Response regulator 3D structure|Response regulator 3D structure]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Cauvi]] | [[Category: Cauvi]] | ||
[[Category: Large Structures]] | |||
[[Category: Cabantous, S]] | [[Category: Cabantous, S]] | ||
[[Category: Guillet, V]] | [[Category: Guillet, V]] |
Revision as of 11:35, 2 December 2020
CRYSTAL STRUCTURE OF THE RESPONSE REGULATOR DIVK AT PH 8.0 IN COMPLEX WITH MN2+CRYSTAL STRUCTURE OF THE RESPONSE REGULATOR DIVK AT PH 8.0 IN COMPLEX WITH MN2+
Structural highlights
Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedDivK 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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