1r5q

<table><tr><td colspan='2'>[[1r5q]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Anabaena_7120 Anabaena 7120]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R5Q OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1R5Q FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Kai A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=103690 Anabaena 7120])</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=1r5q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r5q OCA], [http://pdbe.org/1r5q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1r5q RCSB], [http://www.ebi.ac.uk/pdbsum/1r5q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1r5q ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/KAIA_NOSS1 KAIA_NOSS1]] 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 (By similarity).

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

The cyanobacterial clock proteins KaiA and KaiB are proposed as regulators of the circadian rhythm in cyanobacteria. Mutations in both proteins have been reported to alter or abolish circadian rhythmicity. Here, we present molecular models of both KaiA and KaiB from the cyanobacteria Anabaena sp PCC7120 deduced by crystal structure analysis, and we discuss how clock-changing or abolishing mutations may cause their resulting circadian phenotype. The overall fold of the KaiA monomer is that of a four-helix bundle. KaiB, on the other hand, adopts an alpha-beta meander motif. Both proteins purify and crystallize as dimers. While the folds of the two proteins are clearly different, their size and some surface features of the physiologically relevant dimers are very similar. Notably, the functionally relevant residues Arg 69 of KaiA and Arg 23 of KaiB align well in space. The apparent structural similarities suggest that KaiA and KaiB may compete for a potential common binding site on KaiC.

Anabaena circadian clock proteins KaiA and KaiB reveal a potential common binding site to their partner KaiC.,Garces RG, Wu N, Gillon W, Pai EF EMBO J. 2004 Apr 21;23(8):1688-98. Epub 2004 Apr 8. PMID:15071498<ref>PMID:15071498</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 1r5q" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Anabaena 7120]]

[[Category: Garces, R G]]

[[Category: Gillon, W]]

[[Category: Pai, E F]]

[[Category: Wu, N]]

[[Category: Four-helix-bundle]]

[[Category: Gene regulation]]