Structure of a molecular chaperone from a thermophilic archaebacterium View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1993-02

AUTHORS

Barry M. Phipps, Dieter Typke, Reiner Hegerl, Susanne Volker, Angelika Hoffmann, Karl O. Stetter, Wolfgang Baumeister

ABSTRACT

WE recently reported that a wide range of thermophilic archaebacteria have a novel ATPase complex which accumulates to high levels upon heat shock and may be a new type of molecular chaperone related to the chaperonins1. Striking similarities between the complex, referred to here as the 'thermosome', and the subsequently characterized chaperones TF55 of the thermophilic archaebacterium Sulfolobus shibatae2 and TCP-1 from eukaryotic cytosol2–5 suggest that these proteins belong to a single family. Here we determine the three-dimensional structure of the thermosome from Pyrodictium occultum by random conical tilt reconstruction from electron micrographs. The reconstruction reveals a complex consisting of two rings of eight subunits each, stacked face-to-face. The subunits are kidney-shaped and composed of at least two domains. In the centre of the thermosome is a large cavity of about 6.7 nm diameter; the opening of this cavity on each face of the complex is partially blocked by a mass which appears to be weakly connected to the eight-membered ring. More... »

PAGES

475-477

Journal

TITLE

Nature

ISSUE

6411

VOLUME

361

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/361475a0

DOI

http://dx.doi.org/10.1038/361475a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1004504520


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