2MXX

Structure of Amylase binding Protein A of Streptococcous gordonii: a potential receptor for human salivary amylase enzyme

Summary for 2MXX

• Entry DOI: 10.2210/pdb2mxx/pdb
• NMR Information: BMRB: 25435
• Descriptor: Amylase-binding protein AbpA (1 entity in total)
• Functional Keywords: hydrolase receptor
• Biological source: Streptococcus gordonii str. Challis
• Total number of polymer chains: 1
• Total formula weight: 19170.78

Authors

Sethi, A.,Mohanty, B.,Ramasubbu, N.,Gooley, P.R. (deposition date: 2015-01-18, release date: 2015-05-13, Last modification date: 2024-05-01)

Primary citation

Sethi, A.,Mohanty, B.,Ramasubbu, N.,Gooley, P.R.
Structure of amylase-binding protein A of Streptococcus gordonii: A potential receptor for human salivary alpha-amylase enzyme.
Protein Sci., 24:1013-1018, 2015

PubMed 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. (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.

PubMed: 25739638
DOI: 10.1002/pro.2671

Experimental method

SOLUTION NMR