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 HS P90 family from an aligned set of homologous protein sequences by usin g a transparent method in both manual and automated implementation tha t extracts conformational information from patterns of variation and c onservation within the family. No statistically significant sequence s imilarity relates this family to any protein with known crystal struct ure. However, the secondary structure prediction, together with the as signment 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). (C) 1997 Wiley-Liss, Inc.