pubmed-article:15240481 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:15240481 | lifeskim:mentions | umls-concept:C0376525 | lld:lifeskim |
pubmed-article:15240481 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
pubmed-article:15240481 | lifeskim:mentions | umls-concept:C1704632 | lld:lifeskim |
pubmed-article:15240481 | lifeskim:mentions | umls-concept:C0871261 | lld:lifeskim |
pubmed-article:15240481 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
pubmed-article:15240481 | lifeskim:mentions | umls-concept:C2911692 | lld:lifeskim |
pubmed-article:15240481 | lifeskim:mentions | umls-concept:C1706817 | lld:lifeskim |
pubmed-article:15240481 | lifeskim:mentions | umls-concept:C0376315 | lld:lifeskim |
pubmed-article:15240481 | lifeskim:mentions | umls-concept:C0182953 | lld:lifeskim |
pubmed-article:15240481 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
pubmed-article:15240481 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
pubmed-article:15240481 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:15240481 | pubmed:dateCreated | 2004-7-8 | lld:pubmed |
pubmed-article:15240481 | pubmed:abstractText | 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. | lld:pubmed |
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pubmed-article:15240481 | pubmed:language | eng | lld:pubmed |
pubmed-article:15240481 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15240481 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:15240481 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:15240481 | pubmed:month | Jul | lld:pubmed |
pubmed-article:15240481 | pubmed:issn | 0006-3495 | lld:pubmed |
pubmed-article:15240481 | pubmed:author | pubmed-author:BendeGG | lld:pubmed |
pubmed-article:15240481 | pubmed:author | pubmed-author:Tandeau de... | lld:pubmed |
pubmed-article:15240481 | pubmed:author | pubmed-author:GärtnerWW | lld:pubmed |
pubmed-article:15240481 | pubmed:author | pubmed-author:ScheuflerCC | lld:pubmed |
pubmed-article:15240481 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:15240481 | pubmed:volume | 87 | lld:pubmed |
pubmed-article:15240481 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:15240481 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:15240481 | pubmed:pagination | 476-87 | lld:pubmed |
pubmed-article:15240481 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:15240481 | pubmed:year | 2004 | lld:pubmed |
pubmed-article:15240481 | pubmed:articleTitle | Crystal structures of two cyanobacterial response regulators in apo- and phosphorylated form reveal a novel dimerization motif of phytochrome-associated response regulators. | lld:pubmed |
pubmed-article:15240481 | pubmed:affiliation | Max-Planck-Institut für Biochemie, D-82152 Martinsried, Germany. | lld:pubmed |
pubmed-article:15240481 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:15240481 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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