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

被引：8

作者：

Sethi, Ashish ^{[1
]}

Mohanty, Biswaranjan ^{[2
]}

Ramasubbu, Narayanan ^{[3
]}

Gooley, Paul R. ^{[1
]}

机构：

[1] Univ Melbourne, Mol Sci & Biotechnol Inst Bio21, Dept Biochem & Mol Biol, Parkville, Vic 3010, Australia

[2] Monash Univ, Monash Inst Pharmaceut Sci, Fac Pharm & Pharmaceut Sci, Med Chem, Parkville, Vic 3052, Australia

[3] Rutgers Sch Dent Med, Dept Oral Biol, Newark, NJ 07103 USA

来源：

PROTEIN SCIENCE | 2015年 / 24卷 / 06期

基金：

澳大利亚研究理事会;

关键词：

amylase-binding protein; AbpA; -amylase; NMR; protein structure; NMR STRUCTURE DETERMINATION; TORSION ANGLE DYNAMICS; ALPHA-AMYLASE; ORAL STREPTOCOCCI; BIOFILM FORMATION; GENE ABPA; PROGRAM; IDENTIFICATION; STARCH; SITES;

D O I：

10.1002/pro.2671

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. C-13/ chemical shift and heteronuclear N-15-{H-1} 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 -amylase binding and biofilm formation by streptococci.

引用

页码：1013 / 1018

页数：6

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