1r5p

<StructureSection load='1r5p' size='340' side='right' caption='[[1r5p]], [[Resolution|resolution]] 2.20&Aring;' scene=''>

<table><tr><td colspan='2'>[[1r5p]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Nostoc_sp. Nostoc sp.]. The January 2008 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Circadian Clock Proteins'' by David S. Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2008_1 10.2210/rcsb_pdb/mom_2008_1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R5P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1R5P FirstGlance]. <br>

</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1r5q|1r5q]]</td></tr>

<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KaiB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1180 Nostoc sp.])</td></tr>

<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1r5p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r5p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1r5p RCSB], [http://www.ebi.ac.uk/pdbsum/1r5p PDBsum]</span></td></tr>

<table>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r5/1r5p_consurf.spt"</scriptWhenChecked>

</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].

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== 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>

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*[[Circadian clock protein|Circadian clock protein]]

[[Category: Nostoc sp.]]

[[Category: Garces, R G.]]

[[Category: Gillon, W.]]

[[Category: Pai, E F.]]

[[Category: Wu, N.]]

[[Category: Protein dimer]]