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Structure of amylase‐binding protein A of Streptococcus gordonii : A potential receptor for human salivary α‐amylase enzyme
Author(s) -
Sethi Ashish,
Mohanty Biswaranjan,
Ramasubbu Narayanan,
Gooley Paul R.
Publication year - 2015
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.2671
Subject(s) - streptococcus gordonii , amylase , streptococcus mutans , enzyme , saliva , chemistry , heteronuclear molecule , microbiology and biotechnology , biochemistry , protein structure , streptococcus , biology , bacteria , genetics , stereochemistry , nuclear magnetic resonance spectroscopy
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. 13 Cα/β chemical shift and heteronuclear 15 N‐{ 1 H} 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.