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Bioinformatics and structural characterization of a hypothetical protein from Streptococcus mutans : implication of antibiotic resistance

Nan, Jie LU ; Brostromer, Erik; Liu, Xiang-Yu; Kristensen, Ole and Su, Xiao-Dong LU (2009) In PLoS ONE 4(10). p.7245-7245
Abstract

As an oral bacterial pathogen, Streptococcus mutans has been known as the aetiologic agent of human dental caries. Among a total of 1960 identified proteins within the genome of this organism, there are about 500 without any known functions. One of these proteins, SMU.440, has very few homologs in the current protein databases and it does not fall into any protein functional families. Phylogenetic studies showed that SMU.440 is related to a particular ecological niche and conserved specifically in some oral pathogens, due to lateral gene transfer. The co-occurrence of a MarR protein within the same operon among these oral pathogens suggests that SMU.440 may be associated with antibiotic resistance. The structure determination of SMU.440... (More)

As an oral bacterial pathogen, Streptococcus mutans has been known as the aetiologic agent of human dental caries. Among a total of 1960 identified proteins within the genome of this organism, there are about 500 without any known functions. One of these proteins, SMU.440, has very few homologs in the current protein databases and it does not fall into any protein functional families. Phylogenetic studies showed that SMU.440 is related to a particular ecological niche and conserved specifically in some oral pathogens, due to lateral gene transfer. The co-occurrence of a MarR protein within the same operon among these oral pathogens suggests that SMU.440 may be associated with antibiotic resistance. The structure determination of SMU.440 revealed that it shares the same fold and a similar pocket as polyketide cyclases, which indicated that it is very likely to bind some polyketide-like molecules. From the interlinking structural and bioinformatics studies, we have concluded that SMU.440 could be involved in polyketide-like antibiotic resistance, providing a better understanding of this hypothetical protein. Besides, the combination of multiple methods in this study can be used as a general approach for functional studies of a protein with unknown function.

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Contribution to journal
publication status
published
keywords
Amino Acid Sequence, Bacterial Proteins, Computational Biology, Crystallography, X-Ray, Databases, Protein, Dental Caries, Drug Resistance, Microbial, Gene Transfer, Horizontal, Humans, Ligands, Models, Molecular, Molecular Sequence Data, Phylogeny, Protein Structure, Secondary, Sequence Homology, Amino Acid, Streptococcus mutans
in
PLoS ONE
volume
4
issue
10
pages
7245 - 7245
publisher
Public Library of Science
external identifiers
  • scopus:70350008300
ISSN
1932-6203
DOI
10.1371/journal.pone.0007245
language
English
LU publication?
yes
id
c36b437e-a6d5-41b6-8802-c97e9df1418d
date added to LUP
2016-09-07 22:52:49
date last changed
2017-11-19 04:33:02
@article{c36b437e-a6d5-41b6-8802-c97e9df1418d,
  abstract     = {<p>As an oral bacterial pathogen, Streptococcus mutans has been known as the aetiologic agent of human dental caries. Among a total of 1960 identified proteins within the genome of this organism, there are about 500 without any known functions. One of these proteins, SMU.440, has very few homologs in the current protein databases and it does not fall into any protein functional families. Phylogenetic studies showed that SMU.440 is related to a particular ecological niche and conserved specifically in some oral pathogens, due to lateral gene transfer. The co-occurrence of a MarR protein within the same operon among these oral pathogens suggests that SMU.440 may be associated with antibiotic resistance. The structure determination of SMU.440 revealed that it shares the same fold and a similar pocket as polyketide cyclases, which indicated that it is very likely to bind some polyketide-like molecules. From the interlinking structural and bioinformatics studies, we have concluded that SMU.440 could be involved in polyketide-like antibiotic resistance, providing a better understanding of this hypothetical protein. Besides, the combination of multiple methods in this study can be used as a general approach for functional studies of a protein with unknown function.</p>},
  author       = {Nan, Jie and Brostromer, Erik and Liu, Xiang-Yu and Kristensen, Ole and Su, Xiao-Dong},
  issn         = {1932-6203},
  keyword      = {Amino Acid Sequence,Bacterial Proteins,Computational Biology,Crystallography, X-Ray,Databases, Protein,Dental Caries,Drug Resistance, Microbial,Gene Transfer, Horizontal,Humans,Ligands,Models, Molecular,Molecular Sequence Data,Phylogeny,Protein Structure, Secondary,Sequence Homology, Amino Acid,Streptococcus mutans},
  language     = {eng},
  number       = {10},
  pages        = {7245--7245},
  publisher    = {Public Library of Science},
  series       = {PLoS ONE},
  title        = {Bioinformatics and structural characterization of a hypothetical protein from Streptococcus mutans : implication of antibiotic resistance},
  url          = {http://dx.doi.org/10.1371/journal.pone.0007245},
  volume       = {4},
  year         = {2009},
}