In:
FEBS Letters, Wiley, Vol. 490, No. 1-2 ( 2001-02-09), p. 70-74
Abstract:
Bacillus thuringiensis δ‐endotoxins (Cry proteins), are widely used for insect control and plant protection. They are water‐soluble proteins that insert into membranes forming ion channels. In most Cry toxins α‐helix 2 is broken by a highly conserved proline residue (Pro70 in Cry1Ab), generating a broken‐helix motif. The flexibility of the motif was altered through site‐directed mutagenesis. It was found that increasing the flexibility of the motif decreased the stability, the ion transport ability and the toxicity of the protein. By removing the broken‐helix motif, the biological properties were restored to a wild type level.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1016/S0014-5793(01)02139-1
Language:
English
Publisher:
Wiley
Publication Date:
2001
detail.hit.zdb_id:
212746-5
detail.hit.zdb_id:
1460391-3
SSG:
12