2dql

<table><tr><td colspan='2'>[[2dql]] is a 2 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=2DQL OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2DQL FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=2dql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dql OCA], [http://pdbe.org/2dql PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2dql RCSB], [http://www.ebi.ac.uk/pdbsum/2dql PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2dql ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Pex, a clock-related protein involved in the input pathway of the cyanobacterial circadian clock system, suppresses the expression of clock gene kaiA and lengthens the circadian period. Here, we determined the crystal structure of Anabaena Pex (AnaPex; Anabaena sp. strain PCC 7120) and Synechococcus Pex (SynPex; Synechococcus sp. strain PCC 7942). Pex is a homodimer that forms a winged-helix structure. Using the DNase I protection and electrophoresis mobility shift assays on a Synechococcus kaiA upstream region, we identified a minimal 25-bp sequence that contained an imperfectly inverted repeat sequence as the Pex-binding sequence. Based on crystal structure, we predicted the amino acid residues essential for Pex's DNA-binding activity and examined the effects of various Ala-substitutions in the alpha3 helix and wing region of Pex on in vitro DNA-binding activity and in vivo rhythm functions. Mutant AnaPex proteins carrying a substitution in the wing region displayed no specific DNA-binding activity, whereas those carrying a substitution in the alpha3 helix did display specific binding activity. But the latter were less thermostable than wild-type AnaPex and their in vitro functions were defective. We concluded that Pex binds a kaiA upstream DNA sequence via its wing region and that its alpha3 helix is probably important to its stability.

Functionally important structural elements of the cyanobacterial clock-related protein Pex.,Kurosawa S, Murakami R, Onai K, Morishita M, Hasegawa D, Iwase R, Uzumaki T, Hayashi F, Kitajima-Ihara T, Sakata S, Murakami M, Kouyama T, Ishiura M Genes Cells. 2009 Jan;14(1):1-16. Epub 2008 Nov 21. PMID:19032344<ref>PMID:19032344</ref>

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

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== References ==

<references/>

[[Category: Anabaena 7120]]

[[Category: Kouyama, T]]

[[Category: Kurosawa, S]]

[[Category: Circadian clock associated protein]]

[[Category: Circadian clock protein]]