1suc
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| , resolution 1.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , and | ||||||
| Activity: | Subtilisin, with EC number 3.4.21.62 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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