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- W2079387411 abstract "The structures of two response regulators (RRs) from the cyanobacterium Calothrix PCC7601, RcpA and RcpB, were solved to 1.9- and 1.75-Å 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 ((β/α)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, β5, 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." @default.
- W2079387411 created "2016-06-24" @default.
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- W2079387411 date "2004-07-01" @default.
- W2079387411 modified "2023-10-14" @default.
- W2079387411 title "Crystal Structures of Two Cyanobacterial Response Regulators in Apo- and Phosphorylated Form Reveal a Novel Dimerization Motif of Phytochrome-Associated Response Regulators" @default.
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- W2079387411 doi "https://doi.org/10.1529/biophysj.103.033696" @default.
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