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predicted both hinges, again with multiple false positives. No other predictors had any
success with this.
We believe that the underlying difficulty with this protein stems from the motion itself.
Although we have defined it as a hinge bending motion, arguments for a different
classification are defensible. The domain motions are relatively small, and the hinge
points are quite difficult to define, since the flexibility is distributed among many points.
This is best observed by viewing the animated morph linked to from
molmovdb.org/HAG.
Elastase of pseudomonas aeruginosa
Pseudomonas aeruginosa is an opportunistic bacterial pathogen of humans. Its virulence
stems from the secretion of alkaline protease and elastase. Elastase is a metalloprotease
that cleaves collagen, IgG, IgA, fibronectin, and other proteins as part of its invasive
activity. It is structurally similar to thermolysin, with which it has 28% sequence
identity. Domain hinge bending, with boundaries, was first suggested by Holland et al.
This proved a particularly challenging protein. FO1M and hNMc predicted the hinge in
the open conformer (the latter with multiple false positives.) Only hNMc and hNMd
detected the hinges on the closed conformer, again with false positives. Some of the
difficulty probably lay with the motion itself, which arguably had some shear motion
component. However the primary difficulty is likely to lie with the two bound metals in
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