Characterization of side‐directed mutations in conserved domains of MalK, a bacterial member of the ATP‐binding cassette (ABC) family

FEBS Letters

Schneider, Erwin¹  Wilken, Sylke¹  Walter, Claudia¹ 

[1] Universität Osnabrück, FB Biologie/Chemie, Barbarastr. 11, D-4500 Osnabrück, Germany

关键词: Maltose transport;    MalK;    ATP-binding cassette family;    Site-directed mutagenesis;    Salmonella typhimurium;   

DOI  :  10.1016/0014-5793(92)80473-T

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Site-directed mutagenesis was used to change four amino acid residues (Q82, P152, L179, H192) in the MalK subunit of S. typhimurium maltose transport system which are highly conserved among members of the ATP-binding cassette (ABC) family. Replacement of H192 caused complete failure to complement the transport defect of a malK strain whereas changes of the other residues resulted in reduced or wild-type activity. The purified mutant proteins exhibited ATPase activity comparable to wild-type MalK.

【 授权许可】

Unknown