Chaperone‐assisted expression of authentic bovine adrenodoxin reductase in Escherichia coli

FEBS Letters

Schulz, Georg E²  Ziegler, Gabriele A²  Schweiger, Susann²  Hanukoglu, Israel¹  Vonrhein, Clemens²  Schmidt, Ulrich² 

[1] E. Katzir Biotechnology Program, Research Institute, College of Judea and Samaria, Ariel 44837, Israel;Institut für Organische Chemie und Biochemie, Albert-Ludwigs-Universität, Albertstrasse 21, D-79104 Freiburg im Breisgau, Germany

关键词: Adrenodoxin reductase;    Chaperone coexpression;    Crystallization;    mRNA loop;    Secondary ribosome binding site;   

DOI  :  10.1016/S0014-5793(98)01714-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown