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

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Bioinformatics and structural characterization of a hypothetical protein from Streptococcus mutans : Implication of antibiotic resistance. / Nan, Jie; Brostromer, Erik; Liu, Xiang-Yu; Kristensen, Ole; Su, Xiao-Dong.

In: PLoS ONE, Vol. 4, No. 10, 2009, p. e7245.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Nan, J, Brostromer, E, Liu, X-Y, Kristensen, O & Su, X-D 2009, 'Bioinformatics and structural characterization of a hypothetical protein from Streptococcus mutans: Implication of antibiotic resistance', PLoS ONE, vol. 4, no. 10, pp. e7245. https://doi.org/10.1371/journal.pone.0007245

APA

Nan, J., Brostromer, E., Liu, X-Y., Kristensen, O., & Su, X-D. (2009). Bioinformatics and structural characterization of a hypothetical protein from Streptococcus mutans: Implication of antibiotic resistance. PLoS ONE, 4(10), e7245. https://doi.org/10.1371/journal.pone.0007245

Vancouver

Nan J, Brostromer E, Liu X-Y, Kristensen O, Su X-D. Bioinformatics and structural characterization of a hypothetical protein from Streptococcus mutans: Implication of antibiotic resistance. PLoS ONE. 2009;4(10):e7245. https://doi.org/10.1371/journal.pone.0007245

Author

Nan, Jie ; Brostromer, Erik ; Liu, Xiang-Yu ; Kristensen, Ole ; Su, Xiao-Dong. / Bioinformatics and structural characterization of a hypothetical protein from Streptococcus mutans : Implication of antibiotic resistance. In: PLoS ONE. 2009 ; Vol. 4, No. 10. pp. e7245.

Bibtex

@article{0b0dbb501d5111df8ed1000ea68e967b,
title = "Bioinformatics and structural characterization of a hypothetical protein from Streptococcus mutans: Implication of antibiotic resistance",
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 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.",
keywords = "The Faculty of Pharmaceutical Sciences",
author = "Jie Nan and Erik Brostromer and Xiang-Yu Liu and Ole Kristensen and Xiao-Dong Su",
year = "2009",
doi = "10.1371/journal.pone.0007245",
language = "English",
volume = "4",
pages = "e7245",
journal = "P L o S One",
issn = "1932-6203",
publisher = "Public Library of Science",
number = "10",

}

RIS

TY - JOUR

T1 - Bioinformatics and structural characterization of a hypothetical protein from Streptococcus mutans

T2 - Implication of antibiotic resistance

AU - Nan, Jie

AU - Brostromer, Erik

AU - Liu, Xiang-Yu

AU - Kristensen, Ole

AU - Su, Xiao-Dong

PY - 2009

Y1 - 2009

N2 - 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.

AB - 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.

KW - The Faculty of Pharmaceutical Sciences

U2 - 10.1371/journal.pone.0007245

DO - 10.1371/journal.pone.0007245

M3 - Journal article

VL - 4

SP - e7245

JO - P L o S One

JF - P L o S One

SN - 1932-6203

IS - 10

ER -

ID: 18106015