CHARACTERIZATION OF SIDE-DIRECTED MUTATIONS IN CONSERVED DOMAINS OF MA1K, A BACTERIAL MEMBER OF THE ATP-BINDING CASSETTE (ABC) FAMILY

Autor(en): WALTER, C
WILKEN, S
SCHNEIDER, E 
Stichwörter: ATP-BINDING CASSETTE FAMILY; Biochemistry & Molecular Biology; Biophysics; Cell Biology; CLONING; CYSTIC-FIBROSIS; DNA; ESCHERICHIA-COLI; GENE; MA1K; MALTOSE TRANSPORT; MALTOSE TRANSPORT-SYSTEM; MEMBRANE-COMPONENTS; PROTEINS; REGION; SALMONELLA-TYPHIMURIUM; SEQUENCES; SITE-DIRECTED MUTAGENESIS
Erscheinungsdatum: 1992
Herausgeber: ELSEVIER SCIENCE BV
Journal: FEBS LETTERS
Volumen: 303
Ausgabe: 1
Startseite: 41
Seitenende: 44
Zusammenfassung: 
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.
ISSN: 00145793
DOI: 10.1016/0014-5793(92)80473-T

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