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1k68

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==Crystal Structure of the Phosphorylated Cyanobacterial Phytochrome Response Regulator RcpA==
==Crystal Structure of the Phosphorylated Cyanobacterial Phytochrome Response Regulator RcpA==
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<StructureSection load='1k68' size='340' side='right' caption='[[1k68]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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<StructureSection load='1k68' size='340' side='right'caption='[[1k68]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1k68]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Calothrix_pcc_7601 Calothrix pcc 7601]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K68 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1K68 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1k68]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Tolypothrix_sp._PCC_7601 Tolypothrix sp. PCC 7601]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K68 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K68 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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</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>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PHD:ASPARTYL+PHOSPHATE'>PHD</scene></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PHD:ASPARTYL+PHOSPHATE'>PHD</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1k66|1k66]]</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1k68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k68 OCA], [https://pdbe.org/1k68 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k68 RCSB], [https://www.ebi.ac.uk/pdbsum/1k68 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k68 ProSAT]</span></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AF309559 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1188 Calothrix PCC 7601])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1k68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k68 OCA], [http://pdbe.org/1k68 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1k68 RCSB], [http://www.ebi.ac.uk/pdbsum/1k68 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1k68 ProSAT]</span></td></tr>
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</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q8RTN0_9CYAN Q8RTN0_9CYAN]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k6/1k68_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k6/1k68_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
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</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=1k68 ConSurf].
</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=1k68 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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The structures of two response regulators (RRs) from the cyanobacterium Calothrix PCC7601, RcpA and RcpB, were solved to 1.9- and 1.75-A resolution, respectively. RcpA was found in phosphorylated and RcpB in nonphosphorylated form. Both RRs are members of phytochrome-associated, light-sensing two-component signal transduction pathways, based on histidine kinase-mediated receptor autophosphorylation and phosphorelay to a RR. Despite the overall folding similarity to CheY-type RRs ((beta/alpha)(5)-motif), RcpA and RcpB form homodimers, irrespective of their phosphorylation state, giving insight into a signal transduction putatively different from that of other known RRs. Dimerization is accomplished by a C-terminal extension of the RR polypeptide chain, and the surface formed by H4, beta 5, and H5, which constitute a hydrophobic contact area with distinct interactions between residues of either subunit. Sequence alignments reveal that the identified dimerization motif is archetypal for phytochrome-associated RRs, making them a novel subgroup of CheY-type RRs. The protein structures of RcpA and RcpB are compared to the recently presented protein structure of Rcp1 from Synechocystis.
 
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Crystal structures of two cyanobacterial response regulators in apo- and phosphorylated form reveal a novel dimerization motif of phytochrome-associated response regulators.,Benda C, Scheufler C, Tandeau de Marsac N, Gartner W Biophys J. 2004 Jul;87(1):476-87. PMID:15240481<ref>PMID:15240481</ref>
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==See Also==
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*[[Response regulator 3D structure|Response regulator 3D structure]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1k68" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Calothrix pcc 7601]]
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[[Category: Large Structures]]
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[[Category: Benda, C]]
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[[Category: Tolypothrix sp. PCC 7601]]
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[[Category: Gaertner, W]]
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[[Category: Benda C]]
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[[Category: Marsac, N Tandeau de]]
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[[Category: Gaertner W]]
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[[Category: Scheufler, C]]
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[[Category: Scheufler C]]
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[[Category: Chey homologue]]
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[[Category: Tandeau de Marsac N]]
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[[Category: Homodimer]]
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[[Category: Phosphorylated aspartate]]
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[[Category: Response regulator]]
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[[Category: Signaling protein]]
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Current revision

Crystal Structure of the Phosphorylated Cyanobacterial Phytochrome Response Regulator RcpA

PDB ID 1k68

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