1tf7

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(New page: 200px<br /><applet load="1tf7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tf7, resolution 2.8&Aring;" /> '''Crystal Structure of ...)
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Revision as of 01:05, 21 November 2007


1tf7, resolution 2.8Å

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Crystal Structure of Circadian Clock Protein KaiC

Overview

Circadian (daily) biological clocks express characteristics that are, difficult to explain by known biochemical mechanisms, and will ultimately, require characterizing the structures, functions, and interactions of, their molecular components. KaiC is an essential circadian protein in, cyanobacteria that forms the core of the KaiABC clock protein complex. We, report the crystal structure of the KaiC homohexameric complex at 2.8 A, resolution. The structure resembles a double doughnut with a central pore, that is partially sealed at one end. The crystal structure reveals ATP, binding, inter-subunit organization, a scaffold for Kai-protein complex, formation, the location of critical KaiC mutations, and evolutionary, relationships to other proteins. A key auto-phosphorylation site on KaiC, (T432) is identified from the crystal structure, and mutation of this, residue abolishes circadian rhythmicity. The crystal structure of KaiC, will be essential for understanding this circadian clockwork and for, establishing its links to global gene expression.

About this Structure

1TF7 is a Single protein structure of sequence from Synechococcus sp. with ATP as ligand. Full crystallographic information is available from OCA.

Reference

Visualizing a circadian clock protein: crystal structure of KaiC and functional insights., Pattanayek R, Wang J, Mori T, Xu Y, Johnson CH, Egli M, Mol Cell. 2004 Aug 13;15(3):375-88. PMID:15304218

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