1K66
Crystal Structure of the Cyanobacterial Phytochrome Response Regulator, RcpB
1K66 の概要
| エントリーDOI | 10.2210/pdb1k66/pdb |
| 関連するPDBエントリー | 1K68 |
| 分子名称 | Phytochrome Response Regulator RcpB, BETA-MERCAPTOETHANOL (3 entities in total) |
| 機能のキーワード | response regulator, chey homologue, homodimer, apo-protein, (beta/alpha)5, signaling protein |
| 由来する生物種 | Tolypothrix sp. PCC 7601 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 33670.42 |
| 構造登録者 | Benda, C.,Scheufler, C.,Tandeau de Marsac, N.,Gaertner, W. (登録日: 2001-10-15, 公開日: 2003-12-16, 最終更新日: 2024-02-07) |
| 主引用文献 | Benda, C.,Scheufler, C.,Tandeau de Marsac, N.,Gaertner, W. Crystal structures of two cyanobacterial response regulators in apo- and phosphorylated form reveal a novel dimerization motif of phytochrome-associated response regulators Biophys.J., 87:476-487, 2004 Cited by PubMed Abstract: The structures of two response regulators (RRs) from the cyanobacterium Calothrix PCC7601, RcpA and RcpB, were solved to 1.9- and 1.75-A 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 ((beta/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, beta 5, 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. PubMed: 15240481DOI: 10.1529/biophysj.103.033696 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.75 Å) |
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