1i3c
From Proteopedia
(New page: 200px<br /><applet load="1i3c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i3c, resolution 1.90Å" /> '''RESPONSE REGULATOR F...) |
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| - | [[Image:1i3c.jpg|left|200px]]<br /><applet load="1i3c" size=" | + | [[Image:1i3c.jpg|left|200px]]<br /><applet load="1i3c" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1i3c, resolution 1.90Å" /> | caption="1i3c, resolution 1.90Å" /> | ||
'''RESPONSE REGULATOR FOR CYANOBACTERIAL PHYTOCHROME, RCP1'''<br /> | '''RESPONSE REGULATOR FOR CYANOBACTERIAL PHYTOCHROME, RCP1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The two-component signal transduction pathway widespread in prokaryotes, fungi, molds, and some plants involves an elaborate phosphorelay cascade. | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1I3C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Synechocystis_sp. Synechocystis sp.] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1I3C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Synechocystis_sp. Synechocystis sp.] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I3C OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Synechocystis sp.]] | [[Category: Synechocystis sp.]] | ||
| - | [[Category: Eom, S | + | [[Category: Eom, S H.]] |
| - | [[Category: Im, Y | + | [[Category: Im, Y J.]] |
| - | [[Category: Kang, J | + | [[Category: Kang, J G.]] |
| - | [[Category: Lee, J | + | [[Category: Lee, J Y.]] |
| - | [[Category: Park, C | + | [[Category: Park, C M.]] |
| - | [[Category: Rho, S | + | [[Category: Rho, S H.]] |
| - | [[Category: Song, P | + | [[Category: Song, P S.]] |
| - | [[Category: Yang, S | + | [[Category: Yang, S S.]] |
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: phytochrome]] | [[Category: phytochrome]] | ||
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[[Category: response regulator]] | [[Category: response regulator]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:07:31 2008'' |
Revision as of 11:07, 21 February 2008
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RESPONSE REGULATOR FOR CYANOBACTERIAL PHYTOCHROME, RCP1
Overview
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.
About this Structure
1I3C is a Single protein structure of sequence from Synechocystis sp. with as ligand. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 13:07:31 2008
Categories: Single protein | Synechocystis sp. | Eom, S H. | Im, Y J. | Kang, J G. | Lee, J Y. | Park, C M. | Rho, S H. | Song, P S. | Yang, S S. | SO4 | Phytochrome | Rcp1 | Response regulator
