1SUB
CALCIUM-INDEPENDENT SUBTILISIN BY DESIGN
Summary for 1SUB
| Entry DOI | 10.2210/pdb1sub/pdb |
| Descriptor | SUBTILISIN BPN' CRB-S3, CALCIUM ION, POTASSIUM ION, ... (5 entities in total) |
| Functional Keywords | hydrolase(serine proteinase) |
| Biological source | Bacillus amyloliquefaciens |
| Cellular location | Secreted: P00782 |
| Total number of polymer chains | 1 |
| Total formula weight | 27710.82 |
| Authors | Gallagher, T.,Bryan, P.,Gilliland, G.L. (deposition date: 1992-06-10, release date: 1994-01-31, Last modification date: 2024-10-09) |
| Primary citation | Gallagher, T.,Bryan, P.,Gilliland, G.L. Calcium-independent subtilisin by design. Proteins, 16:205-213, 1993 Cited by PubMed Abstract: 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. PubMed: 8332608DOI: 10.1002/prot.340160207 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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