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

Research output: Contribution to journalArticleResearchpeer-review

4 Citations (Scopus)

Abstract

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
Volume24
Issue number6
DOIs
Publication statusPublished - 2015

Keywords

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

Cite this

@article{0ecb5a65b03f40ff8be0675245bc26c4,
title = "Structure of amylase-binding protein A of Streptococcus gordonii: a potential receptor for human salivary α-amylase enzyme",
abstract = "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.",
keywords = "AbpA, amylase-binding protein, NMR, protein structure, α-amylase",
author = "Ashish Sethi and Biswaranjan Mohanty and Narayanan Ramasubbu and Gooley, {Paul R}",
year = "2015",
doi = "10.1002/pro.2671",
language = "English",
volume = "24",
pages = "1013--1018",
journal = "Protein Science",
issn = "0961-8368",
publisher = "Wiley-Blackwell",
number = "6",

}

Structure of amylase-binding protein A of Streptococcus gordonii: a potential receptor for human salivary α-amylase enzyme. / Sethi, Ashish; Mohanty, Biswaranjan; Ramasubbu, Narayanan; Gooley, Paul R.

In: Protein Science, Vol. 24, No. 6, 2015, p. 1013-1018.

Research output: Contribution to journalArticleResearchpeer-review

TY - JOUR

T1 - Structure of amylase-binding protein A of Streptococcus gordonii: a potential receptor for human salivary α-amylase enzyme

AU - Sethi, Ashish

AU - Mohanty, Biswaranjan

AU - Ramasubbu, Narayanan

AU - Gooley, Paul R

PY - 2015

Y1 - 2015

N2 - 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.

AB - 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.

KW - AbpA

KW - amylase-binding protein

KW - NMR

KW - protein structure

KW - α-amylase

UR - http://onlinelibrary.wiley.com.ezproxy.lib.monash.edu.au/doi/10.1002/pro.2671/epdf

U2 - 10.1002/pro.2671

DO - 10.1002/pro.2671

M3 - Article

VL - 24

SP - 1013

EP - 1018

JO - Protein Science

JF - Protein Science

SN - 0961-8368

IS - 6

ER -