Substrate recognition domains as revealed by active hybrids between the D-arabinitol and ribitol transporters from Klebsiella pneumoniae

Autor(en): Heuel, H
Turgut, S
Schmid, K
Lengeler, JW
Stichwörter: AEROGENES; BINDING; ESCHERICHIA-COLI K-12; GALACTITOL; METABOLISM; Microbiology; MOLECULAR ANALYSIS; NORA GENE; RESISTANCE; STAPHYLOCOCCUS-AUREUS; SUCROSE
Erscheinungsdatum: 1997
Herausgeber: AMER SOC MICROBIOLOGY
Journal: JOURNAL OF BACTERIOLOGY
Volumen: 179
Ausgabe: 19
Startseite: 6014
Seitenende: 6019
Zusammenfassung: 
Two new genes, dalT and rbtT, have been cloned from the dal operon for D-arabinitol and the rbt operon for ribitol uptake and degradation, respectively, in Klebsiella pneumoniae 1033-5P14, derivative KAY2026. Each gene codes for a specific transporter which, based on sequence data, belongs to a large family of carbohydrate transporters which constitutes 12 transmembrane helices, DalT and RbtT show an unusually high similarity (86.2% identical residues for totals of 425 and 427 amino acids, respectively). This allowed the construction of DalT'-Rbt'T and Rbt-T'-Dal'T crossover hybrids by using a natural restriction site overlapping Met202, This site is located within the large cytoplasmic loop which connects the putative helices 6 and 7 and in particular the amino-and the carboxy-terminal halves of the transporters, Both hybrids have close to normal transport activities but essentially the substrate specificities and kinetic properties of the amino-terminal half. This result localizes essential substrate binding and recognition sites to the amino-terminal halves of the proteins in this import-ant class of carbohydrate transporters.
ISSN: 00219193
DOI: 10.1128/jb.179.19.6014-6019.1997

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