1GN2

S123C mutant of the iron-superoxide dismutase from Mycobacterium tuberculosis.

1GN2 の概要

• エントリーDOI: 10.2210/pdb1gn2/pdb
• 分子名称: SUPEROXIDE DISMUTASE, FE (III) ION (2 entities in total)
• 機能のキーワード: oxidoreductase, iron
• 由来する生物種: MYCOBACTERIUM TUBERCULOSIS
• 細胞内の位置: Secreted: P17670
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 185062.17

構造登録者

Bunting, K.A.,Cooper, J.B.,Tickle, I.J.,Young, D.B. (登録日: 2001-10-02, 公開日: 2001-10-05, 最終更新日: 2024-11-13)

主引用文献

Bunting, K.A.,Cooper, J.B.,Tickle, I.J.,Young, D.B.
Engineering of an Intersubunit Disulfide Bridge in the Iron-Superoxide Dismutase of Mycobacterium Tuberculosis.
Arch.Biochem.Biophys., 397:69-, 2002

PubMed Abstract: With the aim of enhancing interactions involved in dimer formation, an intersubunit disulfide bridge was engineered in the superoxide dismutase enzyme of Mycobacterium tuberculosis. Ser-123 was chosen for mutation to cysteine since it resides at the dimer interface where the serine side chain interacts with the same residue in the opposite subunit. Gel electrophoresis and X-ray crystallographic studies of the expressed mutant confirmed formation of the disulfide bond under nonreducing conditions. However, the mutant protein was found to be less stable than the wild type as judged by susceptibility to denaturation in the presence of guanidine hydrochloride. Decreased stability probably results from formation of a disulfide bridge with a suboptimal torsion angle and exclusion of solvent molecules from the dimer interface.

PubMed: 11747311
DOI: 10.1006/ABBI.2001.2635

実験手法

X-RAY DIFFRACTION (3.4 Å)