Caught in the act: how ATP binding triggers cooperative conformational changes in a molecular machine.
A paper recently published in Cell describes ATP-triggered conformational changes in the GroEL folding machine deciphered by use of cryo-electron microscopy, molecular engineering, and X-ray crystallographic data. Mechanistically crucial allosteric effects of ATP binding arise from rearrangement of interdomain electrostatic contacts.
Gierasch
Lila M
LM
Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, MA 01003, USA.
D000255:Adenosine Triphosphate / Q000737:chemistry*; D018834:Chaperonin 60 / Q000737:chemistry* / Q000648:ultrastructure; D020285:Cryoelectron Microscopy; D004926:Escherichia coli; D008958:Models, Molecular; D020409:Molecular Motor Proteins; D011485:Protein Binding; D017510:Protein Folding
D018834:Chaperonin 60; D020409:Molecular Motor Proteins; D000255:Adenosine Triphosphate