Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Gutsche, I. et al.

Gutsche, Holzinger, Rössle, Heumann, Baumeister, May,

Conformational rearrangements of an archaeal chaperonin upon ATPase cycling.

Chaperonins are double-ring protein assemblies with a central cavity that provides a sequestered environment for in vivo protein folding. Their reaction cycle is thought to consist of a nucleotide-regulated alternation between an open substrate-acceptor state and a closed folding-active state. The cavity of ATP-charged group I chaperonins, typified by Escherichia coli GroEL [1], is sealed off by a co-chaperonin, whereas group II chaperonins--the archaeal thermosome and eukaryotic TRiC/ CCT [2]--possess a built-in lid [3-5]. The mechanism of the lid's rearrangements requires clarification, as even in the absence of nucleotides, thermosomes of Thermoplama acidophilum appear open in vitrified ice [6] and closed in crystals [4]. Here we analyze the conformation of the thermosome at each step of the ATPase cycle by small-angle neutron scattering. The apo-chaperonin is open in solution, and ATP binding induces its further expansion. Closure seems to occur during ATP hydrolysis and before phosphate release, and represents the rate-limiting step of the cycle. The same closure can be triggered by the crystallization buffer. Thus, the allosteric regulation of group II chaperonins appears different from that of their group I counterparts.[1]

References

Conformational rearrangements of an archaeal chaperonin upon ATPase cycling. Gutsche, I., Holzinger, J., Rössle, M., Heumann, H., Baumeister, W., May, R.P. Curr. Biol. (2000) [Pubmed]

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