1suy
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(New page: 200px<br /><applet load="1suy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1suy" /> '''NMR structure of the ThKaiA180C-CIIABD compl...)
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Revision as of 00:34, 21 November 2007
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NMR structure of the ThKaiA180C-CIIABD complex (average minimized structure)
Overview
Circadian clocks are widespread endogenous mechanisms that control the, temporal pattern of diverse biological processes, including gene, transcription. KaiA is the positive element of the cyanobacterial clock, because KaiA overexpression elevates transcription levels of clock, components. Recently, we showed that the structure of KaiA is that of a, domain-swapped homodimer. The N-terminal domain is a pseudo-receiver;, thus, it is likely to be involved in signal transduction in the, clock-resetting pathway. The C-terminal domain of KaiA is structurally, novel and enhances the KaiC autokinase activity directly. Here, we report, the NMR structure of the C-terminal domain of KaiA (ThKaiA180C) in complex, with a KaiC-derived peptide from the cyanobacterium Thermosynechococcus, elongatus BP-1. The protein-peptide interface is revealed to be different, from a model that was proposed earlier, is stabilized by a combination of, hydrophobic and electrostatic interactions, and includes many residues, known to produce a circadian-period phenotype upon substitution. Although, the structure of the monomeric subunit of ThKaiA180C is largely unchanged, upon peptide binding, the intersubunit dimerization angle changes. It is, proposed that modulation of the C-terminal KaiA domain dimerization angle, regulates KaiA-KaiC interactions.
About this Structure
1SUY is a Protein complex structure of sequences from Bacteria. Full crystallographic information is available from OCA.
Reference
Structure of the C-terminal domain of the clock protein KaiA in complex with a KaiC-derived peptide: implications for KaiC regulation., Vakonakis I, LiWang AC, Proc Natl Acad Sci U S A. 2004 Jul 27;101(30):10925-30. Epub 2004 Jul 15. PMID:15256595
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