2qke
From Proteopedia
(New page: '''Unreleased structure''' The entry 2qke is ON HOLD until Paper Publication Authors: Pattanayek, R., Egli, M., Pattanayek, S. Description: Wild Type Crystal Structure of Full Length C...) |
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| + | {{STRUCTURE_2qke| PDB=2qke | SCENE= }} | ||
| - | + | '''Wild Type Crystal Structure of Full Length Circadian Clock Protein KaiB from Thermosynechococcus elongatus BP-1''' | |
| - | Description: Wild Type Crystal Structure of Full Length Circadian Clock Protein KaiB from Thermosynechococcus elongatus BP-1 | ||
| + | ==Overview== | ||
| + | The circadian clock of the cyanobacterium Synechococcus elongatus can be reconstituted in vitro by the KaiA, KaiB and KaiC proteins in the presence of ATP. The principal clock component, KaiC, undergoes regular cycles between hyper- and hypo-phosphorylated states with a period of ca. 24 h that is temperature compensated. KaiA enhances KaiC phosphorylation and this enhancement is antagonized by KaiB. Throughout the cycle Kai proteins interact in a dynamic manner to form complexes of different composition. We present a three-dimensional model of the S. elongatus KaiB-KaiC complex based on X-ray crystallography, negative-stain and cryo-electron microscopy, native gel electrophoresis and modelling techniques. We provide experimental evidence that KaiB dimers interact with KaiC from the same side as KaiA and for a conformational rearrangement of the C-terminal regions of KaiC subunits. The enlarged central channel and thus KaiC subunit separation in the C-terminal ring of the hexamer is consistent with KaiC subunit exchange during the dephosphorylation phase. The proposed binding mode of KaiB explains the observation of simultaneous binding of KaiA and KaiB to KaiC, and provides insight into the mechanism of KaiB's antagonism of KaiA. | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun | + | ==About this Structure== |
| + | 2QKE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Synechococcus_elongatus Synechococcus elongatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QKE OCA]. | ||
| + | |||
| + | ==Reference== | ||
| + | Structural model of the circadian clock KaiB-KaiC complex and mechanism for modulation of KaiC phosphorylation., Pattanayek R, Williams DR, Pattanayek S, Mori T, Johnson CH, Stewart PL, Egli M, EMBO J. 2008 May 22;. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18497745 18497745] | ||
| + | [[Category: Single protein]] | ||
| + | [[Category: Synechococcus elongatus]] | ||
| + | [[Category: Egli, M.]] | ||
| + | [[Category: Pattanayek, R.]] | ||
| + | [[Category: Pattanayek, S.]] | ||
| + | [[Category: Cyanobacterial circadian clock protein]] | ||
| + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 18 12:03:21 2008'' | ||
Revision as of 09:03, 18 June 2008
Wild Type Crystal Structure of Full Length Circadian Clock Protein KaiB from Thermosynechococcus elongatus BP-1
Overview
The circadian clock of the cyanobacterium Synechococcus elongatus can be reconstituted in vitro by the KaiA, KaiB and KaiC proteins in the presence of ATP. The principal clock component, KaiC, undergoes regular cycles between hyper- and hypo-phosphorylated states with a period of ca. 24 h that is temperature compensated. KaiA enhances KaiC phosphorylation and this enhancement is antagonized by KaiB. Throughout the cycle Kai proteins interact in a dynamic manner to form complexes of different composition. We present a three-dimensional model of the S. elongatus KaiB-KaiC complex based on X-ray crystallography, negative-stain and cryo-electron microscopy, native gel electrophoresis and modelling techniques. We provide experimental evidence that KaiB dimers interact with KaiC from the same side as KaiA and for a conformational rearrangement of the C-terminal regions of KaiC subunits. The enlarged central channel and thus KaiC subunit separation in the C-terminal ring of the hexamer is consistent with KaiC subunit exchange during the dephosphorylation phase. The proposed binding mode of KaiB explains the observation of simultaneous binding of KaiA and KaiB to KaiC, and provides insight into the mechanism of KaiB's antagonism of KaiA.
About this Structure
2QKE is a Single protein structure of sequence from Synechococcus elongatus. Full crystallographic information is available from OCA.
Reference
Structural model of the circadian clock KaiB-KaiC complex and mechanism for modulation of KaiC phosphorylation., Pattanayek R, Williams DR, Pattanayek S, Mori T, Johnson CH, Stewart PL, Egli M, EMBO J. 2008 May 22;. PMID:18497745 Page seeded by OCA on Wed Jun 18 12:03:21 2008
