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
收藏
页码：1013 / 1018
页数：6
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