Prediction of the structural similarity between spermidine/putrescine-binding protein and maltose-binding protein.
A structural similarity between spermidine/putrescine-binding protein and maltose-binding protein has been predicted by a sequence-structure compatibility method. The sequence alignment obtained by this method revealed a consensus sequence motif located on the surface loop between the first alpha-helix and the second beta-strand, and the further analysis identified a similar motif in iron-binding protein. The conservation of this motif among certain bacterial periplasmic binding proteins suggests a common functional role for this region as well as an evolutionary relationship between them.
Matsuo
Y
Y
Protein Engineering Research Institute, Osaka, Japan.
Nishikawa
K
K
D018528:ATP-Binding Cassette Transporters; D000595:Amino Acid Sequence; D002352:Carrier Proteins / Q000737:chemistry*; D016384:Consensus Sequence; D004926:Escherichia coli / Q000737:chemistry*; D029968:Escherichia coli Proteins; D058619:Maltose-Binding Proteins; D026901:Membrane Transport Proteins; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009004:Monosaccharide Transport Proteins; D033902:Periplasmic Binding Proteins; D016415:Sequence Alignment / Q000379:methods; D017386:Sequence Homology, Amino Acid
D018528:ATP-Binding Cassette Transporters; D002352:Carrier Proteins; D029968:Escherichia coli Proteins; C461619:MalE protein, E coli; D058619:Maltose-Binding Proteins; D026901:Membrane Transport Proteins; D009004:Monosaccharide Transport Proteins; D033902:Periplasmic Binding Proteins; C099274:PotD protein, E coli; C461599:maltose transport system, E coli