1v2z

From Proteopedia

(Difference between revisions)

Revision as of 06:23, 6 October 2021

Crystal structure of the C-terminal domain of Thermosynechococcus elongatus BP-1 KaiA

Structural highlights

1v2z is a 1 chain structure with sequence from Theeb. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

[KAIA_THEEB] Component of the KaiABC clock protein complex, which constitutes the main circadian regulator in cyanobacteria. The KaiABC complex may act as a promoter-nonspecific transcription regulator that represses transcription, possibly by acting on the state of chromosome compaction. In the complex, it enhances the phosphorylation status of KaiC. In contrast, the presence of KaiB in the complex decreases the phosphorylation status of KaiC, suggesting that KaiB acts by antagonizing the interaction between KaiA and KaiC. A KaiA dimer is sufficient to enhance KaiC hexamer phosphorylation.

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

KaiA, KaiB and KaiC constitute the circadian clock machinery in cyanobacteria, and KaiA activates kaiBC expression whereas KaiC represses it. Here we show that KaiA is composed of three functional domains, the N-terminal amplitude-amplifier domain, the central period-adjuster domain and the C-terminal clock-oscillator domain. The C-terminal domain is responsible for dimer formation, binding to KaiC, enhancing KaiC phosphorylation and generating the circadian oscillations. The X-ray crystal structure at a resolution of 1.8 A of the C-terminal clock-oscillator domain of KaiA from the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1 shows that residue His270, located at the center of a KaiA dimer concavity, is essential to KaiA function. KaiA binding to KaiC probably occurs via the concave surface. On the basis of the structure, we predict the structural roles of the residues that affect circadian oscillations.

Crystal structure of the C-terminal clock-oscillator domain of the cyanobacterial KaiA protein.,Uzumaki T, Fujita M, Nakatsu T, Hayashi F, Shibata H, Itoh N, Kato H, Ishiura M Nat Struct Mol Biol. 2004 Jul;11(7):623-31. Epub 2004 May 30. PMID:15170179^[1]

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

References

↑ Uzumaki T, Fujita M, Nakatsu T, Hayashi F, Shibata H, Itoh N, Kato H, Ishiura M. Crystal structure of the C-terminal clock-oscillator domain of the cyanobacterial KaiA protein. Nat Struct Mol Biol. 2004 Jul;11(7):623-31. Epub 2004 May 30. PMID:15170179 doi:10.1038/nsmb781

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/1v2z"

@@ Line 3: / Line 3: @@
 <StructureSection load='1v2z' size='340' side='right'caption='[[1v2z]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1v2z]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Theeb Theeb]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V2Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1V2Z FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1v2z]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Theeb Theeb]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V2Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V2Z FirstGlance]. <br>
-</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=1v2z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v2z OCA], [http://pdbe.org/1v2z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1v2z RCSB], [http://www.ebi.ac.uk/pdbsum/1v2z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1v2z ProSAT], [http://www.topsan.org/Proteins/RSGI/1v2z TOPSAN]</span></td></tr>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1v2z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v2z OCA], [https://pdbe.org/1v2z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v2z RCSB], [https://www.ebi.ac.uk/pdbsum/1v2z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v2z ProSAT], [https://www.topsan.org/Proteins/RSGI/1v2z TOPSAN]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/KAIA_THEEB KAIA_THEEB]] Component of the KaiABC clock protein complex, which constitutes the main circadian regulator in cyanobacteria. The KaiABC complex may act as a promoter-nonspecific transcription regulator that represses transcription, possibly by acting on the state of chromosome compaction. In the complex, it enhances the phosphorylation status of KaiC. In contrast, the presence of KaiB in the complex decreases the phosphorylation status of KaiC, suggesting that KaiB acts by antagonizing the interaction between KaiA and KaiC. A KaiA dimer is sufficient to enhance KaiC hexamer phosphorylation.
+[[https://www.uniprot.org/uniprot/KAIA_THEEB KAIA_THEEB]] Component of the KaiABC clock protein complex, which constitutes the main circadian regulator in cyanobacteria. The KaiABC complex may act as a promoter-nonspecific transcription regulator that represses transcription, possibly by acting on the state of chromosome compaction. In the complex, it enhances the phosphorylation status of KaiC. In contrast, the presence of KaiB in the complex decreases the phosphorylation status of KaiC, suggesting that KaiB acts by antagonizing the interaction between KaiA and KaiC. A KaiA dimer is sufficient to enhance KaiC hexamer phosphorylation.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1v2z

From Proteopedia

Revision as of 06:23, 6 October 2021

Crystal structure of the C-terminal domain of Thermosynechococcus elongatus BP-1 KaiA

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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