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Crystal Structure Of The Archaeal Chaperonin Thermosome, A Protein-Folding Machine, Determined

e molecular level seems to differ considerably as only group I chaperonins depend on a second, smaller kind of protein, the cochaperonins 10, termed GroES in E. coli. These helper molecules are not present in the group II system. Whereas detailed structural studies were available for group I chaperonins, including the atomic model of the GroEL-GroES complex, such structural information was not available for members of group II. The crystal structure of the thermosome provides clues for understanding the mode of action of group II chaperonins on a molecular basis, containing a built-in lid domain that substitutes for a cochaperonin.


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Contact: Robert Huber
huber@biochem.mpg.de
+49-89-85782678
Max-Planck-Gesellschaft
3-Apr-1998


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