2qke

From Proteopedia

(Difference between revisions)

Revision as of 07:06, 10 June 2020

Wild Type Crystal Structure of Full Length Circadian Clock Protein KaiB from Thermosynechococcus elongatus BP-1

Structural highlights

2qke is a 6 chain structure with sequence from Synechococcus elongatus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1vgl, 1r5p, 1wwj
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[KAIB_THEEB] Component of the KaiABC clock protein complex, which constitutes the main circadian regulator in cyanobacteria. The KaiABC complex may act as a promoter-non-specific transcription regulator that represses transcription, possibly by acting on the state of chromosome compaction. In the complex, it decreases the phosphorylation status of KaiC. It has no effect on KaiC by itself, but instead needs the presence of both KaiA and KaiC, suggesting that it acts by antagonizing the interaction between KaiA and KaiC.[HAMAP-Rule:MF_01835]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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 Jun 18;27(12):1767-78. Epub 2008 May 22. PMID:18497745^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Pattanayek R, Williams DR, Pattanayek S, Mori T, Johnson CH, Stewart PL, Egli M. Structural model of the circadian clock KaiB-KaiC complex and mechanism for modulation of KaiC phosphorylation. EMBO J. 2008 Jun 18;27(12):1767-78. Epub 2008 May 22. PMID:18497745 doi:10.1038/emboj.2008.104

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2qke"

@@ Line 1: / Line 1: @@
 ==Wild Type Crystal Structure of Full Length Circadian Clock Protein KaiB from Thermosynechococcus elongatus BP-1==
-<StructureSection load='2qke' size='340' side='right' caption='[[2qke]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
+<StructureSection load='2qke' size='340' side='right'caption='[[2qke]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2qke]] is a 6 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2QKE FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2qke]] is a 6 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2QKE FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1vgl|1vgl]], [[1r5p|1r5p]], [[1wwj|1wwj]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qke FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qke OCA], [http://pdbe.org/2qke PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2qke RCSB], [http://www.ebi.ac.uk/pdbsum/2qke PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2qke ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2qke FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qke OCA], [http://pdbe.org/2qke PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2qke RCSB], [http://www.ebi.ac.uk/pdbsum/2qke PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2qke ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 30: / Line 30: @@
 ==See Also==
-*[[Circadian clock protein|Circadian clock protein]]
+*[[Circadian clock protein 3D structures|Circadian clock protein 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Synechococcus elongatus]]
 [[Category: Egli, M]]

2qke

From Proteopedia

Revision as of 07:06, 10 June 2020

Wild Type Crystal Structure of Full Length Circadian Clock Protein KaiB from Thermosynechococcus elongatus BP-1

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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