1k66
From Proteopedia
(New page: 200px<br /><applet load="1k66" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k66, resolution 1.75Å" /> '''Crystal Structure of...) |
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| - | [[Image:1k66.jpg|left|200px]]<br /><applet load="1k66" size=" | + | [[Image:1k66.jpg|left|200px]]<br /><applet load="1k66" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1k66, resolution 1.75Å" /> | caption="1k66, resolution 1.75Å" /> | ||
'''Crystal Structure of the Cyanobacterial Phytochrome Response Regulator, RcpB'''<br /> | '''Crystal Structure of the Cyanobacterial Phytochrome Response Regulator, RcpB'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structures of two response regulators (RRs) from the cyanobacterium | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1K66 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Tolypothrix_sp._pcc_7601 Tolypothrix sp. pcc 7601] with BME as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1K66 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Tolypothrix_sp._pcc_7601 Tolypothrix sp. pcc 7601] with <scene name='pdbligand=BME:'>BME</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K66 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Benda, C.]] | [[Category: Benda, C.]] | ||
[[Category: Gaertner, W.]] | [[Category: Gaertner, W.]] | ||
| - | [[Category: Marsac, N | + | [[Category: Marsac, N Tandeau de.]] |
[[Category: Scheufler, C.]] | [[Category: Scheufler, C.]] | ||
[[Category: BME]] | [[Category: BME]] | ||
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[[Category: response regulator]] | [[Category: response regulator]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:30:32 2008'' |
Revision as of 11:30, 21 February 2008
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Crystal Structure of the Cyanobacterial Phytochrome Response Regulator, RcpB
Overview
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.
About this Structure
1K66 is a Single protein structure of sequence from Tolypothrix sp. pcc 7601 with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structures of two cyanobacterial response regulators in apo- and phosphorylated form reveal a novel dimerization motif of phytochrome-associated response regulators., Benda C, Scheufler C, Tandeau de Marsac N, Gartner W, Biophys J. 2004 Jul;87(1):476-87. PMID:15240481
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