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Chaperone‐assisted expression of authentic bovine adrenodoxin reductase in Escherichia coli
Author(s) -
Vonrhein Clemens,
Schmidt Ulrich,
Ziegler Gabriele A,
Schweiger Susann,
Hanukoglu Israel,
Schulz Georg E
Publication year - 1999
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/s0014-5793(98)01714-1
Subject(s) - adrenodoxin , escherichia coli , chaperone (clinical) , biochemistry , ribosome , reductase , biology , chemistry , microbiology and biotechnology , enzyme , gene , cytochrome , medicine , rna , pathology
Adrenodoxin reductase is an essential component of the mitochondrial monooxygenase systems that are involved in the synthesis of steroid hormones and related compounds. After removing by mutagenesis a secondary ribosome binding site and an mRNA loop formed between the gene and the vector, large amounts of the enzyme could be produced in Escherichia coli by coexpression with the HSP60‐chaperone system. The purified protein was homogeneous enough for reproducible crystallization. The crystals diffracted X‐rays isotropically beyond 1.7 Å resolution permitting a structure analysis.