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Structure of the C-terminal domain of the surface antigen SpaP from the caries pathogen Streptococcus mutans
SpaP is a 1500-residue adhesin expressed on the surface of the caries-implicated bacterium Streptococcus mutans. SpaP is a member of the antigen I/II (AgI/II) family of proteins expressed by oral streptococci. These surface proteins are crucial for the incorporation of streptococci into dental plaqu...
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Formato: | Texto |
Lenguaje: | English |
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International Union of Crystallography
2010
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3079964/ https://www.ncbi.nlm.nih.gov/pubmed/21206016 http://dx.doi.org/10.1107/S174430911004443X |
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author | Nylander, Åsa Forsgren, Nina Persson, Karina |
author_facet | Nylander, Åsa Forsgren, Nina Persson, Karina |
author_sort | Nylander, Åsa |
collection | PubMed |
description | SpaP is a 1500-residue adhesin expressed on the surface of the caries-implicated bacterium Streptococcus mutans. SpaP is a member of the antigen I/II (AgI/II) family of proteins expressed by oral streptococci. These surface proteins are crucial for the incorporation of streptococci into dental plaque. The structure of the C-terminal domain of SpaP (residues 1136–1489) was solved and refined to 2.2 Å resolution with six molecules in the asymmetric unit. Similar to a related AgI/II structure, SpaP is stabilized by isopeptide bonds between lysine and asparagine side chains. |
format | Text |
id | pubmed-3079964 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
spelling | pubmed-30799642011-04-20 Structure of the C-terminal domain of the surface antigen SpaP from the caries pathogen Streptococcus mutans Nylander, Åsa Forsgren, Nina Persson, Karina Acta Crystallogr Sect F Struct Biol Cryst Commun Structural Communications SpaP is a 1500-residue adhesin expressed on the surface of the caries-implicated bacterium Streptococcus mutans. SpaP is a member of the antigen I/II (AgI/II) family of proteins expressed by oral streptococci. These surface proteins are crucial for the incorporation of streptococci into dental plaque. The structure of the C-terminal domain of SpaP (residues 1136–1489) was solved and refined to 2.2 Å resolution with six molecules in the asymmetric unit. Similar to a related AgI/II structure, SpaP is stabilized by isopeptide bonds between lysine and asparagine side chains. International Union of Crystallography 2010-12-21 /pmc/articles/PMC3079964/ /pubmed/21206016 http://dx.doi.org/10.1107/S174430911004443X Text en © Nylander et al. 2011 http://creativecommons.org/licenses/by/2.0/uk/ This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited. |
spellingShingle | Structural Communications Nylander, Åsa Forsgren, Nina Persson, Karina Structure of the C-terminal domain of the surface antigen SpaP from the caries pathogen Streptococcus mutans |
title | Structure of the C-terminal domain of the surface antigen SpaP from the caries pathogen Streptococcus mutans
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title_full | Structure of the C-terminal domain of the surface antigen SpaP from the caries pathogen Streptococcus mutans
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title_fullStr | Structure of the C-terminal domain of the surface antigen SpaP from the caries pathogen Streptococcus mutans
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title_full_unstemmed | Structure of the C-terminal domain of the surface antigen SpaP from the caries pathogen Streptococcus mutans
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title_short | Structure of the C-terminal domain of the surface antigen SpaP from the caries pathogen Streptococcus mutans
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title_sort | structure of the c-terminal domain of the surface antigen spap from the caries pathogen streptococcus mutans |
topic | Structural Communications |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3079964/ https://www.ncbi.nlm.nih.gov/pubmed/21206016 http://dx.doi.org/10.1107/S174430911004443X |
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