Structural aspects of GroEL function.
The chaperonin GroEL and its cofactor GroES facilitate protein folding in an ATP-regulated manner. The recently solved crystal structure of the GroEL.GroES.(ADP)7 complex shows that the lining of the cavity in the polypeptide acceptor state is hydrophobic, whereas in the protein-release state it becomes hydrophilic. Other highlights of the past year include the visualization of the allosteric states of GroEL with respect to ATP using cryo-electron microscopy, and an X-ray crystallographic analysis of the interaction between the apical domain of GroEL and a peptide.
Horovitz
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Department of Structural Biology, Weizmann Institute, Rehovot, Israel. csamnon@weizmann.weizmann.ac.il
D000255:Adenosine Triphosphate / Q000378:metabolism; D018834:Chaperonin 60 / Q000737:chemistry* / Q000378:metabolism*; D015925:Cryopreservation; D018360:Crystallography, X-Ray; D008854:Microscopy, Electron; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D017510:Protein Folding
D018834:Chaperonin 60; D010455:Peptides; D000255:Adenosine Triphosphate