5c5e: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Structure of KaiA dimer in complex with C-terminal KaiC peptide at 2.8 A resolution== | ==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]] 2.82Å' scene=''> | <StructureSection load='5c5e' size='340' side='right'caption='[[5c5e]], [[Resolution|resolution]] 2.82Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5c5e]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Anacystis_nidulans_r2 Anacystis nidulans r2]. 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> | <table><tr><td colspan='2'>[[5c5e]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Anacystis_nidulans_r2 Anacystis nidulans r2]. 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> | ||
| Line 19: | Line 19: | ||
</div> | </div> | ||
<div class="pdbe-citations 5c5e" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5c5e" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Circadian clock protein 3D structures|Circadian clock protein 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 24: | Line 27: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Anacystis nidulans r2]] | [[Category: Anacystis nidulans r2]] | ||
[[Category: Large Structures]] | |||
[[Category: Egli, M]] | [[Category: Egli, M]] | ||
[[Category: Pattanayek, R]] | [[Category: Pattanayek, R]] | ||
[[Category: Clock protein kaia-kaic complex]] | [[Category: Clock protein kaia-kaic complex]] | ||
[[Category: Transcription]] | [[Category: Transcription]] | ||
Revision as of 14:09, 25 December 2019
Structure of KaiA dimer in complex with C-terminal KaiC peptide at 2.8 A resolutionStructure of KaiA dimer in complex with C-terminal KaiC peptide at 2.8 A resolution
Structural highlights
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 PubMedIn 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. See AlsoReferences
|
| ||||||||||||||||||