Autor: |
Narayanan Ramasubbu, Ashish Sethi, Biswaranjan Mohanty, Paul R. Gooley |
Rok vydání: |
2015 |
Předmět: |
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Zdroj: |
Protein Science. 24:1013-1018 |
ISSN: |
0961-8368 |
DOI: |
10.1002/pro.2671 |
Popis: |
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. 13Cα/β chemical shift and heteronuclear 15N-{1H} 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. |
Databáze: |
OpenAIRE |
Externí odkaz: |
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