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Biophysical Journal 87:476-487 (2004)
© 2004 The Biophysical Society

Crystal Structures of Two Cyanobacterial Response Regulators in Apo- and Phosphorylated Form Reveal a Novel Dimerization Motif of Phytochrome-Associated Response Regulators

C. Benda * {dagger}, C. Scheufler {dagger}, N. Tandeau de Marsac {ddagger} and W. Gärtner * §

* Max-Planck-Institut für Biochemie, D-82152 Martinsried, Germany; {dagger} Proteros Biostructures GmbH, D-82152 Planegg-Martinsried, Germany; {ddagger} Unité des Cyanobactéries (CNRS URA 2172), Institut Pasteur, 75728 Paris, Cedex 15, France; and § Max-Planck-Institut für Bioanorganische Chemie, D-45470 Mülheim, Germany

Correspondence: Address reprint requests to W. Gärtner, Max-Planck-Institut für Bioanorganische Chemie, D-45470 Mülheim, Germany. E-mail: gaertner{at}mpi-muelheim.mpg.de.

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 ((ß/{alpha})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, ß5, 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.




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