In:
FEBS Letters, Wiley, Vol. 279, No. 2 ( 1991-02-25), p. 240-242
Abstract:
Wheat germ contains an inhibitor for proicinase K, called PK13 ( M 1 ∼ 19600) which simultaneously inhibits α‐amylase. PK13 was crystallized, space group P 2 1 , α = 43.02 (5) Å, n = 65.18 (7) Å, c = 32.33 (4) Å, β = 112.79 (9), X‐ray data were collected to 2.5 Å resolution, the structure solved by molecular replacement on the basis of the atomic coordinates of the homologous Erythrina caffra DE‐3 inhibitor, and refined with simulated annealing techniques with a current R‐factor of 21%. The three‐dimensional structure of PK13 is stabilized by two disulfide bridges and has a central β‐barrel with distorted β‐structure. In analogy to related inhibitors, the binding site for proteinase K is assumed to be located on the surface of the protein (amino acids residues 66–67), although the 75–76 peptide bond is cleaved upon binding.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1016/0014-5793(91)80158-Y
Language:
English
Publisher:
Wiley
Publication Date:
1991
detail.hit.zdb_id:
1460391-3
SSG:
12
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