Structural highlights
Publication Abstract from PubMed
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 Calpha/beta 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 alpha-amylase binding and biofilm formation by streptococci.
Structure of amylase-binding protein A of Streptococcus gordonii: A potential receptor for human salivary alpha-amylase enzyme.,Sethi A, Mohanty B, Ramasubbu N, Gooley PR Protein Sci. 2015 Mar 4. doi: 10.1002/pro.2671. PMID:25739638[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sethi A, Mohanty B, Ramasubbu N, Gooley PR. Structure of amylase-binding protein A of Streptococcus gordonii: A potential receptor for human salivary alpha-amylase enzyme. Protein Sci. 2015 Mar 4. doi: 10.1002/pro.2671. PMID:25739638 doi:http://dx.doi.org/10.1002/pro.2671
