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A model for the secondary structure of β‐lactamases
Author(s) -
Bunster Marta,
Cid Hilda
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80749-8
Subject(s) - bacillus licheniformis , bacillus cereus , escherichia coli , enzyme , protein secondary structure , staphylococcus aureus , chemistry , sequence (biology) , domain (mathematical analysis) , function (biology) , microbiology and biotechnology , computational biology , biological system , biology , biochemistry , bacteria , bacillus subtilis , genetics , mathematics , mathematical analysis , gene
A 3‐dimensional model, common for the secondary structures of four β‐lactamases obtained from Escherichia coli , Bacillus licheniformis , Bacillus cereus and Staphylococcus aureus , is proposed. The predictions of the structures were made by the hydrophobicity profiles method complemented by the modified Chou and Fasman's method. The model proposed presents 56% constancy and can be described as a 2‐domain structure, in agreement with low resolution X‐ray data reported for the E. coli enzyme. The model would explain how a common function can be performed by enzymes of very different sizes, composition and sequence.