Crystal structure of a cyanobacterial phytochrome response regulator.
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.
Im
Young Jun
YJ
Department of Life Science, Kwangju Institute of Science and Technology, Kwangju 500-712, Korea.
Rho
Seong-Hwan
SH
Park
Chung-Mo
CM
Yang
Song-Sook
SS
Kang
Jeong-Gu
JG
Lee
Jae Young
JY
Song
Pill-Soon
PS
Eom
Soo Hyun
SH
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry; D001665:Binding Sites; D000458:Cyanobacteria / Q000737:chemistry* / Q000502:physiology; D019281:Dimerization; D008345:Manganese / Q000737:chemistry / Q000378:metabolism; D008565:Membrane Proteins / Q000737:chemistry; D000072236:Methyl-Accepting Chemotaxis Proteins; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010766:Phosphorylation; D020283:Photoreceptors, Microbial; D010834:Phytochrome / Q000737:chemistry / Q000502:physiology; D011487:Protein Conformation; D011494:Protein Kinases / Q000737:chemistry / Q000502:physiology; D011506:Proteins / Q000737:chemistry*; D015398:Signal Transduction
D001426:Bacterial Proteins; D008565:Membrane Proteins; D000072236:Methyl-Accepting Chemotaxis Proteins; D020283:Photoreceptors, Microbial; D011506:Proteins; C107945:Rcp1 protein, Synechocystis; D010834:Phytochrome; D008345:Manganese; D011494:Protein Kinases; C413623:Cph1 phytochrome protein, bacteria