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
相关论文
共 50 条
  • [41] 3-DIMENSIONAL STRUCTURE OF HUMAN SALIVARY ALPHA-AMYLASE
    RAMASUBBU, N
    VENUGOPALAN, P
    LEVINE, MJ
    JOURNAL OF DENTAL RESEARCH, 1995, 74 : 483 - 483
  • [42] Human salivary α-amylase:: Roles of histidines in the starch hydrolysis and bacterial binding.
    Miyamoto, M
    Ramasubbu, N
    Ramalingam, K
    Levine, MJ
    FASEB JOURNAL, 1997, 11 (09): : A1033 - A1033
  • [43] THE BINDING OF HUMAN SALIVARY ALPHA-AMYLASE BY ORAL STRAINS OF STREPTOCOCCAL BACTERIA
    DOUGLAS, CWI
    ARCHIVES OF ORAL BIOLOGY, 1983, 28 (07) : 567 - 573
  • [44] RECEPTOR-MEDIATED PINOCYTOSIS OF GLYCOSYLATED HUMAN SALIVARY AMYLASE BY RAT MACROPHAGES
    NIESEN, TE
    ALPERS, DH
    ROSENBLUM, JL
    GASTROENTEROLOGY, 1983, 84 (05) : 1261 - 1261
  • [45] PURIFICATION AND CHARACTERIZATION OF ALPHA-AMYLASE-BINDING TRYPTIC FRAGMENTS FROM STREPTOCOCCUS-GORDONII G9B
    ROGERS, JD
    SCANNAPIECO, FA
    JOURNAL OF DENTAL RESEARCH, 1995, 74 : 249 - 249
  • [46] Alpha-amylase is a human salivary protein with affinity to lipopolysaccharide of Aggregatibacter actinomycetemcomitans
    Baik, J. E.
    Hong, S. W.
    Choi, S.
    Jeon, J. H.
    Park, O. -J.
    Cho, K.
    Seo, D. -G.
    Kum, K. -Y.
    Yun, C-H.
    Han, S. H.
    MOLECULAR ORAL MICROBIOLOGY, 2013, 28 (02) : 142 - 153
  • [47] Structure-function relationships in human salivary α-amylase:: role of aromatic residues
    Ramasubbu, N
    Ragunath, C
    Sundar, K
    Mishra, PJ
    Gyémánt, G
    Kandra, L
    BIOLOGIA, 2005, 60 : 47 - 56
  • [48] Sour cherry extract inhibits human salivary α-amylase and growth of Streptococcus mutans (a pilot clinical study)
    Homoki, Judit
    Gyemant, Gyongyi
    Balogh, Peter
    Stundl, Laszlo
    Biro-Molnar, Piroska
    Paholcsek, Melinda
    Varadi, Judit
    Ferenc, Fenyvesi
    Kelentey, Barna
    Nemes, Judit
    Remenyik, Judit
    FOOD & FUNCTION, 2018, 9 (07) : 4008 - 4016
  • [49] Human salivary α-amylase Trp58 situated at subsite -2 is critical for enzyme activity
    Ramasubbu, N
    Ragunath, C
    Mishra, PJ
    Thomas, LM
    Gyémánt, G
    Kandra, L
    EUROPEAN JOURNAL OF BIOCHEMISTRY, 2004, 271 (12): : 2517 - 2529
  • [50] DNA-binding activities in Streptococcus gordonii: Identification of a receptor-nickase and a histonelike protein
    Lunsford, RD
    Nguyen, N
    London, J
    CURRENT MICROBIOLOGY, 1996, 32 (02) : 95 - 100
12345