Machinery of protein folding and unfolding.
During the past two years, a large amount of biochemical, biophysical and low- to high-resolution structural data have provided mechanistic insights into the machinery of protein folding and unfolding. It has emerged that dual functionality in terms of folding and unfolding might exist for some systems. The majority of folding/unfolding machines adopt oligomeric ring structures in a cooperative fashion and utilise the conformational changes induced by ATP binding/hydrolysis for their specific functions.
Zhang
Xiaodong
X
Centre for Structural Biology, Department of Biological Sciences, Imperial College of Science, Technology and Medicine, Flowers Building, South Kensington, SW7 2AZ, London, UK. xiaodong.zhang@ic.ac.uk
Beuron
Fabienne
F
Freemont
Paul S
PS
D000255:Adenosine Triphosphate / Q000378:metabolism; D002352:Carrier Proteins / Q000737:chemistry / Q000378:metabolism; D018835:Chaperonin 10 / Q000737:chemistry / Q000378:metabolism; D018834:Chaperonin 60 / Q000737:chemistry / Q000378:metabolism; D056404:Chaperonin Containing TCP-1; D018833:Chaperonins / Q000737:chemistry* / Q000378:metabolism*; D029968:Escherichia coli Proteins; D018840:HSP70 Heat-Shock Proteins / Q000737:chemistry / Q000378:metabolism; D018841:HSP90 Heat-Shock Proteins / Q000737:chemistry / Q000378:metabolism; D006868:Hydrolysis; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000737:chemistry* / Q000378:metabolism*; D052066:N-Ethylmaleimide-Sensitive Proteins; D017510:Protein Folding; D033921:Vesicular Transport Proteins
D002352:Carrier Proteins; D018835:Chaperonin 10; D018834:Chaperonin 60; D029968:Escherichia coli Proteins; D018840:HSP70 Heat-Shock Proteins; D018841:HSP90 Heat-Shock Proteins; D018832:Molecular Chaperones; D033921:Vesicular Transport Proteins; C112806:prefoldin; D000255:Adenosine Triphosphate; D056404:Chaperonin Containing TCP-1; D018833:Chaperonins; C063842:dnaK protein, E coli; D052066:N-Ethylmaleimide-Sensitive Proteins