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[...]on page 623 of this issue1, Flaherty et al. suggest that major conformational changes play an important part in the function of heat-shock proteins, on the basis of the extensive structural similarity they observe between the ATPbinding domains of the heat-shock protein hsp70 and the enzyme hex...

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Bibliographic Details
Published in:Nature (London) 1990-08, Vol.346 (6285), p.607-608
Main Author: Branden, Carl-Iver
Format: Article
Language:English
Subjects:
Adenosine triphosphatase
ATP
Binding
Chaperones
Clathrin
Coated vesicles
Enzymes
Guanosine triphosphate
Heat shock proteins
Hexokinase
Hsp60 protein
Hsp70 protein
NAD
Polypeptides
Protein folding
Proteins
Strands
Substrates
Uncoating
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Summary:[...]on page 623 of this issue1, Flaherty et al. suggest that major conformational changes play an important part in the function of heat-shock proteins, on the basis of the extensive structural similarity they observe between the ATPbinding domains of the heat-shock protein hsp70 and the enzyme hexokinase, the archetypal example of an enzyme activated by 'induced fit' when a substrate is bound. [...]the NAD-binding domains of several dehydrogenases4 have six parallel /З-strands in a specific arrangement, the Rossmann fold (c in the figure), and GTP-binding proteins5 form a family of structures containing five parallel and one antiparallel /З-strands (b in the figure), the G-protein fold. If this were so, perhaps a similar ATPase fold will be found in other ATP-dependent chaperones, such as8 GroE, a member of the hsp60 chaperonin family. Because the complete structure of the uncoating ATPase remains unknown, it is as yet impossible to say how the energy released by the hydrolysis of ATP is used to liberate clathrin molecules from coated vesicles.
ISSN:0028-0836
1476-4687
DOI:10.1038/346607a0