What is it about?
Circadian (daily) protein clocks are found in cyanobacteria, where a complex of the KaiA, KaiB and KaiC proteins generates circadian rhythms. The 28.09 kDa KaiC homologue PH0284 protein from Pyrococcus horikoshii OT3 was cloned and expressed and the purified protein was crystallized by the oil-microbatch method at 295 K. X-ray diffraction data from the crystal were collected to 2.0 A resolution using synchrotron radiation at 100 K.
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Why is it important?
We report the expression, purification and preliminary crystallographic analysis of the RecA superfamily ATPase PH0284 and its complex with ATP.
Perspectives
Circadian clocks are self-sustained biochemical oscillators. Their properties include a time constant of approximately 24 h (daily cycle) and accurate temperature compensation. In the circadian-clock machinery found in cyanobacteria, direct protein–protein inter- actions between the KaiA, KaiB and KaiC proteins may be a critical process in the generation of circadian rhythms through cyclic regu- lation of gene expression (Ishiura et al., 1998). A RecA superfamily protein, KaiC, is the core component of the clock-protein complex KaiABC (Johnson, 2004). Recently, KaiC homologous proteins have also been found in archaea as RecA superfamily ATPases (Johnson & Golden, 1999; Dvornyk et al., 2003). Most of the archaeal RecA superfamily ATPases are hypothetical and more than one copy is sometimes found.
Dr Bagautdin Bagautdinov
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This page is a summary of: Purification, crystallization and preliminary crystallographic analysis of RecA superfamily ATPase PH0284 fromPyrococcus horikoshiiOT3, Acta Crystallographica Section F Structural Biology and Crystallization Communications, March 2006, International Union of Crystallography,
DOI: 10.1107/s1744309106009973.
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