Structure of amylase-binding protein A of Streptococcus gordonii: a potential receptor for human salivary α-amylase enzyme

Ashish Sethi, Biswaranjan Mohanty, Narayanan Ramasubbu, Paul R Gooley

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6 Citations (Scopus)


Amylase-binding protein A (AbpA) of a number of oral streptococci is essential for the colonization of the dental pellicle. We have determined the solution structure of residues 24-195 of AbpA of Streptococcus gordonii and show a well-defined core of five helices in the region of 45-115 and 135-145. 13Cα/β chemical shift and heteronuclear 15N-{1H} NOE data are consistent with this fold and that the remainder of the protein is unstructured. The structure will inform future molecular experiments in defining the mechanism of human salivary α-amylase binding and biofilm formation by streptococci.
Original languageEnglish
Pages (from-to)1013-1018
Number of pages6
JournalProtein Science
Issue number6
Publication statusPublished - 2015


  • AbpA
  • amylase-binding protein
  • NMR
  • protein structure
  • α-amylase

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