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Crystal structure of a cyanobacterial phytochrome response regulator

Cited 17 time in Web of Science Cited 17 time in Scopus
Authors
Im, Young Jun; Rho, Seong-Hwan; Park, Chung-Mo; Yang, Song-Sook; Kang, Jeong-Gu; Lee, Jae Young; Song, Pill-Soon; Eom, Soo Hyun
Issue Date
2002-03
Citation
Protein Science, Vol.11 No.3, pp.614-624
Keywords
response regulatortwo-component systemcyanobacterial phytochromeRcp1
Abstract
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 Angstrom. The structure reveals a tightly associated hemodimer 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.
ISSN
0961-8368
URI
https://hdl.handle.net/10371/172095
DOI
https://doi.org/10.1110/ps.39102
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College of Natural Sciences (자연과학대학)Dept. of Chemistry (화학부)Journal Papers (저널논문_화학부)
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