5c5e

From Proteopedia

(Difference between revisions)

Revision as of 16:05, 17 May 2017

Structure of KaiA dimer in complex with C-terminal KaiC peptide at 2.8 A resolution

Structural highlights

5c5e is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[KAIA_SYNE7] 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.^[1] ^[2] ^[3] ^[4]

Publication Abstract from PubMed

In the cyanobacterial circadian clock, the KaiA, -B, and -C proteins with ATP constitute a post-translational oscillator. KaiA stimulates the KaiC autokinase, and KaiB antagonizes KaiA action. KaiA contacts the intrinsically disordered C-terminal regions of KaiC hexamer to promote phosphorylation across subunit interfaces. The crystal structure of KaiA dimer from Synechococcus elongatus with two KaiC C-terminal 20mer peptides bound reveals that the latter adopt an alpha-helical conformation and contact KaiA alpha-helical bundles via mostly hydrophobic interactions. This complex and the crystal structure of KaiC hexamer with truncated C-terminal tails can be fit into the electron microscopy (EM) density of the KaiA:KaiC complex. The hybrid model helps rationalize clock phenotypes of KaiA and KaiC mutants.

Protein-Protein Interactions in the Cyanobacterial Circadian Clock: Structure of KaiA Dimer in Complex with C-Terminal KaiC Peptides at 2.8 A Resolution.,Pattanayek R, Egli M Biochemistry. 2015 Aug 4;54(30):4575-8. doi: 10.1021/acs.biochem.5b00694. Epub, 2015 Jul 24. PMID:26200123^[5]

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

References

↑ Iwasaki H, Nishiwaki T, Kitayama Y, Nakajima M, Kondo T. KaiA-stimulated KaiC phosphorylation in circadian timing loops in cyanobacteria. Proc Natl Acad Sci U S A. 2002 Nov 26;99(24):15788-93. Epub 2002 Oct 21. PMID:12391300 doi:http://dx.doi.org/10.1073/pnas.222467299
↑ Xu Y, Mori T, Johnson CH. Cyanobacterial circadian clockwork: roles of KaiA, KaiB and the kaiBC promoter in regulating KaiC. EMBO J. 2003 May 1;22(9):2117-26. PMID:12727878 doi:10.1093/emboj/cdg168
↑ Kitayama Y, Iwasaki H, Nishiwaki T, Kondo T. KaiB functions as an attenuator of KaiC phosphorylation in the cyanobacterial circadian clock system. EMBO J. 2003 May 1;22(9):2127-34. PMID:12727879 doi:10.1093/emboj/cdg212
↑ Ishiura M, Kutsuna S, Aoki S, Iwasaki H, Andersson CR, Tanabe A, Golden SS, Johnson CH, Kondo T. Expression of a gene cluster kaiABC as a circadian feedback process in cyanobacteria. Science. 1998 Sep 4;281(5382):1519-23. PMID:9727980
↑ Pattanayek R, Egli M. Protein-Protein Interactions in the Cyanobacterial Circadian Clock: Structure of KaiA Dimer in Complex with C-Terminal KaiC Peptides at 2.8 A Resolution. Biochemistry. 2015 Aug 4;54(30):4575-8. doi: 10.1021/acs.biochem.5b00694. Epub, 2015 Jul 24. PMID:26200123 doi:http://dx.doi.org/10.1021/acs.biochem.5b00694

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5c5e"

Categories: Egli, M | Pattanayek, R | Clock protein kaia-kaic complex | Transcription

@@ Line 1: / Line 1: @@
 ==Structure of KaiA dimer in complex with C-terminal KaiC peptide at 2.8 A resolution==
 <StructureSection load='5c5e' size='340' side='right' caption='[[5c5e]], [[Resolution|resolution]] 2.82&Aring;' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[5c5e]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C5E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5C5E FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=52M:2-(6-HYDROXY-3-OXO-3H-XANTHEN-9-YL)-5-[(SULFANYLCARBONYL)AMINO]BENZOIC+ACID'>52M</scene></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=5c5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c5e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5c5e RCSB], [http://www.ebi.ac.uk/pdbsum/5c5e PDBsum]</span></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=5c5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c5e OCA], [http://pdbe.org/5c5e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c5e RCSB], [http://www.ebi.ac.uk/pdbsum/5c5e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5c5e ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 16: / Line 17: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 5c5e" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Circadian clock protein|Circadian clock protein]]
 == References ==
 <references/>

5c5e

From Proteopedia

Revision as of 16:05, 17 May 2017

Structure of KaiA dimer in complex with C-terminal KaiC peptide at 2.8 A resolution

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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