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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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Detalles Bibliográficos
Autores principales: Nylander, Åsa, Forsgren, Nina, Persson, Karina
Formato: Texto
Lenguaje:English
Publicado: International Union of Crystallography 2010
Materias:
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.
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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
title_full Structure of the C-terminal domain of the surface antigen SpaP from the caries pathogen Streptococcus mutans
title_fullStr Structure of the C-terminal domain of the surface antigen SpaP from the caries pathogen Streptococcus mutans
title_full_unstemmed Structure of the C-terminal domain of the surface antigen SpaP from the caries pathogen Streptococcus mutans
title_short Structure of the C-terminal domain of the surface antigen SpaP from the caries pathogen Streptococcus mutans
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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