1suc
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CALCIUM-INDEPENDENT SUBTILISIN BY DESIGN
OverviewOverview
A version of subtilisin BPN' lacking the high affinity calcium site (site, A) has been produced through genetic engineering methods, and its crystal, structure refined at 1.8 A resolution. This protein and the corresponding, version containing the calcium A site are described and compared. The, deletion of residues 75-83 was made in the context of four site-specific, replacements previously shown to stabilize subtilisin. The helix that in, wild type is interrupted by the calcium binding loop, is continuous in the, deletion mutant, with normal geometry. A few residues adjacent to the, loop, principally those that were involved in calcium coordination, are, repositioned and/or destabilized by the deletion. Because refolding is, greatly facilitated by the absence of the Ca-loop, this protein offers a, new vehicle for analysis and dissection of the folding reaction. This is, among the largest internal changes to a protein to be described at atomic, resolution.
About this StructureAbout this Structure
1SUC is a Single protein structure of sequence from Bacillus amyloliquefaciens with K, CYA and ACN as ligands. Active as Subtilisin, with EC number 3.4.21.62 Full crystallographic information is available from OCA.
ReferenceReference
Calcium-independent subtilisin by design., Gallagher T, Bryan P, Gilliland GL, Proteins. 1993 Jun;16(2):205-13. PMID:8332608
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