Structure and function of a model member of the SulP transporter family.
SHST1 is a sulfate transporter that belongs to a large and diverse family of anion transporters. Little is known about the structure and function of any member of the family. Site-directed mutagenesis of SHST1 is being used to understand the function of particular amino acids. We have mutated highly conserved amino acid residues and the results suggest that the first two helices play an important role in the transport pathway. Furthermore, mutation of equivalent residues to those altered in human genetic diseases produces deleterious effects in SHST1. These results suggest that there are similarities in the molecular mechanism of transport throughout the family and the information obtained with SHST1 may be applicable to the entire family.
School of Biochemistry and Molecular Biology, Faculty of Science, Australian National University, Canberra, ACT.
Patrick
P
Loughlin
Megan C
MC
Shelden
M Louise
ML
Tierney
Susan M
SM
Howitt
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry; D001692:Biological Transport; D002352:Carrier Proteins / Q000737:chemistry / Q000378:metabolism*; D017124:Conserved Sequence; D007887:Fabaceae; D008956:Models, Chemical; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D010940:Plant Proteins / Q000737:chemistry; D017433:Protein Structure, Secondary; D013329:Structure-Activity Relationship; D013431:Sulfates / Q000378:metabolism
D000596:Amino Acids; D002352:Carrier Proteins; D010940:Plant Proteins; D013431:Sulfates