1vgl
From Proteopedia
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'''Crystal structure of tetrameric KaiB from T.elongatus BP-1''' | '''Crystal structure of tetrameric KaiB from T.elongatus BP-1''' | ||
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[[Category: Namba, K.]] | [[Category: Namba, K.]] | ||
[[Category: Uzumaki, T.]] | [[Category: Uzumaki, T.]] | ||
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Revision as of 09:31, 3 May 2008
Crystal structure of tetrameric KaiB from T.elongatus BP-1
Overview
KaiB is a component of the circadian clock oscillator in cyanobacteria, which are the simplest organisms that exhibit circadian rhythms. KaiB consists of 108 amino-acid residues and has a molecular weight of 12 025 Da. KaiB and Cys-substituted KaiB mutants from the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1 were expressed as GST-fusion proteins in Escherichia coli, purified and crystallized. The crystals of wild-type KaiB belong to the monoclinic space group P2(1), with unit-cell parameters a = 89.6, b = 71.2, c = 106.8 A, beta = 100.1 degrees. While the native crystals diffract to 3.7 A, osmium derivatives, which show an approximately 4 A shrinkage in the b axis, diffract to 2.6 A. The crystals of the singly Cys-substituted mutant T64C with Hg, which show different morphology, diffract to 2.5 A and belong to the monoclinic space group P2, with unit-cell parameters a = 63.7, b = 33.4, c = 93.7 A, beta = 100.1 degrees. Anomalous difference Patterson maps of the Os- and Hg-derivative crystals had significant peaks in their Harker sections, suggesting that both derivatives are suitable for structure determination.
About this Structure
1VGL is a Single protein structure of sequence from Bacteria. Full crystallographic information is available from OCA.
Reference
Crystallization and preliminary crystallographic analysis of the circadian clock protein KaiB from the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1., Iwase R, Imada K, Hayashi F, Uzumaki T, Namba K, Ishiura M, Acta Crystallogr D Biol Crystallogr. 2004 Apr;60(Pt 4):727-9. Epub 2004, Mar 23. PMID:15039567 Page seeded by OCA on Sat May 3 12:31:07 2008
