Structural similarities between chaperone molecules of the HSP60 and HSP70 families deduced from hydrophobic cluster analysis.
In this study, the conservation of strong structural landmarks between all the members of two chaperone families (HSP60 and HSP70) was deduced from their sequences by hydrophobic cluster analysis. On this basis, we propose that the ATP-binding environment is maintained by a similar fold in both protein families. The observed similarities extend throughout the proteins, including both the ATPase domain and the C-terminal substrate-binding domain.
Callebaut
I
I
Département des Macromolécules Biologiques, CNRS URA09, Universités Paris VI-Paris, France.
Catelli
M G
MG
Portetelle
D
D
Burny
A
A
Baulieu
E E
EE
Mornon
J P
JP
D000251:Adenosine Triphosphatases / Q000737:chemistry / Q000648:ultrastructure; D000255:Adenosine Triphosphate / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry / Q000648:ultrastructure; D001665:Binding Sites; D018833:Chaperonins; D006360:Heat-Shock Proteins / Q000737:chemistry* / Q000648:ultrastructure; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry* / Q000648:ultrastructure; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D001426:Bacterial Proteins; D006360:Heat-Shock Proteins; D011506:Proteins; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases; D018833:Chaperonins