4g86 | pdb_00004g86

Crystal structure of the redox-active cofactor DBMIB bound to the full length circadian clock protein KaiA from Synechococcus elongatus

spinqualitylabelsall models 4g86, resolution 2.39Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4g86 is a 2 chain structure with sequence from Synechococcus elongatus pcc 7942. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 1PE, 2PE, BNT, GOL Related: 1r8j Gene: kaiA, see0009, Synpcc7942_1218 (Synechococcus elongatus PCC 7942) Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed KaiA protein that stimulates KaiC phosphorylation in the cyanobacterial circadian clock was recently shown to be destabilized by dibromothymoquinone (DBMIB), thus revealing KaiA as a sensor of the plastoquinone (PQ) redox state and suggesting an indirect control of the clock by light through PQ redox changes. Here we show using X-ray crystallography that several DBMIBs are bound to KaiA dimer. Some binding modes are consistent with oligomerization of N-terminal KaiA pseudoreceiver domains and/or reduced interdomain flexibility. DBMIB bound to the C-terminal KaiA (C-KaiA) domain and limited stimulation of KaiC kinase activity by C-KaiA in the presence of DBMIB demonstrate that the cofactor may weakly inhibit KaiA-KaiC binding. Crystal Structure of the Redox-Active Cofactor Dibromothymoquinone Bound to Circadian Clock Protein KaiA and Structural Basis for Dibromothymoquinone's Ability to Prevent Stimulation of KaiC Phosphorylation by KaiA.,Pattanayek R, Sidiqi SK, Egli M Biochemistry. 2012 Oct 5. PMID:23020633 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Circadian clock protein

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