January 2023
Volume 299Issue 1
Open Access
On the Cover: Hsp17 is a member of the family of small heat shock proteins in C.elegans.
It protects the proteome as a molecular chaperone. In the article by Strauch et al.,
the structure and mechanism of Hsp17 is reported. The cryo EM structure revealed a
sphere composed of 24 subunits shown in the cover as snowflakes. In this structure,
12 of the N-terminal segments are oriented towards the interior while the other 12
point outside. The later ones are engaged in interactions with substrate proteins.
The snowflakes represent soluble Hsp17 complexes present in large quantities in the
cell. They can also be engaged in insoluble aggregates as shown at the bottom of the
figure...Show more
On the Cover: Hsp17 is a member of the family of small heat shock proteins in C.elegans.
It protects the proteome as a molecular chaperone. In the article by Strauch et al.,
the structure and mechanism of Hsp17 is reported. The cryo EM structure revealed a
sphere composed of 24 subunits shown in the cover as snowflakes. In this structure,
12 of the N-terminal segments are oriented towards the interior while the other 12
point outside. The later ones are engaged in interactions with substrate proteins.
The snowflakes represent soluble Hsp17 complexes present in large quantities in the
cell. They can also be engaged in insoluble aggregates as shown at the bottom of the
figure
