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Low resolution crystal structures of Taka-amylase A and its complexes with inhibitors.

Authors :
Matsuura Y
Kusunoki M
Date W
Harada S
Bando S
Tanaka N
Kakudo M
Source :
Journal of biochemistry [J Biochem] 1979 Dec; Vol. 86 (6), pp. 1773-83.
Publication Year :
1979

Abstract

The molecular structure of Taka-amylase A, an alpha-amylase from Aspergillus oryzae, has been studied at 6 A resolution by X-ray diffraction analysis. The electron density map showed a non-crystallographic three-fold screw arrangement of the molecules in the crystal. The molecule is an ellipsoid with approximate dimensions of 80 x 45 x 35 A and contains a hollow which may correspond to the active center. The inhibitor molecules bind to Taka-amylase A at four different sites, one of which is located in the hollow of the enzyme. The probable position of a thiol group is discussed in connection with heavy atom binding.

Details

Language :
English
ISSN :
0021-924X
Volume :
86
Issue :
6
Database :
MEDLINE
Journal :
Journal of biochemistry
Publication Type :
Academic Journal
Accession number :
93603
Full Text :
https://doi.org/10.1093/oxfordjournals.jbchem.a132699