2zfw

Crystal structure of Pex from Synechococcus sp. (strain PCC 7942) (Anacystis nidulans R2)

spinqualitylabelsall models 2zfw, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2zfw is a 4 chain structure with sequence from Synechococcus sp.. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SO4 Related: 2dql Gene: pex (Synechococcus sp.) Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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