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Title
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X-ray analysis and circular dichroism of the acid protease from Endothia parasitica and chymosin.
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Authors
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J.Jenkins,
I.Tickle,
T.Sewell,
L.Ungaretti,
A.Wollmer,
T.Blundell.
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Ref.
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Adv Exp Med Biol, 1977,
95,
43-60.
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PubMed id
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Abstract
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The structure of an acid proteinase from Endothia parasitica has been solved by
x-ray diffraction using multiple isomorphous replacement. A 3 A resolution map
was interpreted in terms of a bilobal structure with a long 25 A cleft. The
secondary structure is mostly distorted beta-sheet. The circular dichroism was
measured and model curves for different secondary structures were fitted by
least squares indicating a large component of beta-structure. The structure was
seen to be homologous with that of the acid proteinase from R. Chinensis and
hence with pepsin and chymosin. A rotation function against diffraction data
from chymosin crystals confirm confirm this and suggested an approach to the
solution of this structure.
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