1m2f | pdb_00001m2f

Solution structure of the N-terminal domain of Synechococcus elongatus KaiA (KaiA135N); Family of 25 structures

spinqualitylabelsall models 1m2f, 25 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1m2f is a 1 chain structure with sequence from Pcc 6301. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1m2e Gene: KaiA (PCC 6301) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [KAIA_SYNE7] 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. 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 In the cyanobacterium Synechococcus elongatus (PCC 7942) the proteins KaiA, KaiB, and KaiC are required for circadian clock function. We deduced a circadian clock function for KaiA from a combination of biochemical and structural data. Both KaiA and its isolated carboxyl-terminal domain (KaiA180C) stimulated KaiC autophosphorylation and facilitated attenuation of KaiC autophosphorylation by KaiB. An amino-terminal domain (KaiA135N) had no function in the autophosphorylation assay. NMR structure determination showed that KaiA135N is a pseudo-receiver domain. We propose that this pseudo-receiver is a timing input-device that regulates KaiA stimulation of KaiC autophosphorylation, which in turn is essential for circadian timekeeping. Structure and function from the circadian clock protein KaiA of Synechococcus elongatus: a potential clock input mechanism.,Williams SB, Vakonakis I, Golden SS, LiWang AC Proc Natl Acad Sci U S A. 2002 Nov 26;99(24):15357-62. Epub 2002 Nov 15. PMID:12438647 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Circadian clock protein 3D structures

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