1i3c

<table><tr><td colspan='2'>[[1i3c]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aphanocapsa_sp._(strain_n-1) Aphanocapsa sp. (strain n-1)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I3C OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1I3C FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>

<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SLR0474 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1148 Aphanocapsa sp. (strain N-1)])</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=1i3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i3c OCA], [http://pdbe.org/1i3c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1i3c RCSB], [http://www.ebi.ac.uk/pdbsum/1i3c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1i3c ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/RCP1_SYNY3 RCP1_SYNY3]] Forms a two-component system with cph1 in which it acts as receiver substrate.

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== Publication Abstract from PubMed ==

The two-component signal transduction pathway widespread in prokaryotes, fungi, molds, and some plants involves an elaborate phosphorelay cascade. Rcp1 is the phosphate receiver module in a two-component system controlling the light response of cyanobacteria Synechocystis sp. via cyanobacterial phytochrome Cph1, which recognizes Rcp1 and transfers its phosphoryl group to an aspartate residue in response to light. Here we describe the crystal structure of Rcp1 refined to a crystallographic R-factor of 18.8% at a resolution of 1.9 A. The structure reveals a tightly associated homodimer with monomers comprised of doubly wound five-stranded parallel beta-sheets forming a single-domain protein homologous with the N-terminal activator domain of other response regulators (e.g., chemotaxis protein CheY). The three-dimensional structure of Rcp1 appears consistent with the conserved activation mechanism of phosphate receiver proteins, although in this case, the C-terminal half of its regulatory domain, which undergoes structural changes upon phosphorylation, contributes to the dimerization interface. The involvement of the residues undergoing phosphorylation-induced conformational changes at the dimeric interface suggests that dimerization of Rcp1 may be regulated by phosphorylation, which could affect the interaction of Rcp1 with downstream target molecules.

Crystal structure of a cyanobacterial phytochrome response regulator.,Im YJ, Rho SH, Park CM, Yang SS, Kang JG, Lee JY, Song PS, Eom SH Protein Sci. 2002 Mar;11(3):614-24. PMID:11847283<ref>PMID:11847283</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1i3c" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Eom, S H]]

[[Category: Im, Y J]]

[[Category: Kang, J G]]

[[Category: Lee, J Y]]

[[Category: Park, C M]]

[[Category: Rho, S H]]

[[Category: Song, P S]]

[[Category: Yang, S S]]

[[Category: Signaling protein]]