A predicted consensus structure for the N-terminal fragment of the heat shock protein HSP90 family.
A secondary structure has been predicted for the heat shock protein HSP90 family from an aligned set of homologous protein sequences by using a transparent method in both manual and automated implementation that extracts conformational information from patterns of variation and conservation within the family. No statistically significant sequence similarity relates this family to any protein with known crystal structure. However, the secondary structure prediction, together with the assignment of active site positions and possible biochemical properties, suggest that the fold is similar to that seen in N-terminal domain of DNA gyrase B (the ATPase fragment).
Gerloff
D L
DL
Department of Cellular, University of California, San Francisco, USA.
Cohen
F E
FE
Korostensky
C
C
Turcotte
M
M
Gonnet
G H
GH
Benner
S A
SA
D000465:Algorithms; D001665:Binding Sites; D027081:DNA Gyrase; D004250:DNA Topoisomerases, Type II / Q000737:chemistry / Q000378:metabolism; D018841:HSP90 Heat-Shock Proteins / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
D018841:HSP90 Heat-Shock Proteins; D027081:DNA Gyrase; D004250:DNA Topoisomerases, Type II