Publication

The three-dimensional structure of the nitrogen regulatory protein IIA(Ntr) from Escherichia coli

Bordo, D., Monfort, R. L. M. V., Pijning, T., Kalk, K. H., Reizer, J., Saier Jr., M. H. & Dijkstra, B. W., 29-May-1998, In : Journal of Molecular Biology. 279, 1, p. 245-255 11 p.

Research output: Contribution to journalArticleAcademicpeer-review

APA

Bordo, D., Monfort, R. L. M. V., Pijning, T., Kalk, K. H., Reizer, J., Saier Jr., M. H., & Dijkstra, B. W. (1998). The three-dimensional structure of the nitrogen regulatory protein IIA(Ntr) from Escherichia coli. Journal of Molecular Biology, 279(1), 245-255. https://doi.org/10.1006/jmbi.1998.1753

Author

Bordo, Domenico ; Monfort, Rob L.M. van ; Pijning, Tjaard ; Kalk, Kor H. ; Reizer, Jonathan ; Saier Jr., Milton H. ; Dijkstra, Bauke W. / The three-dimensional structure of the nitrogen regulatory protein IIA(Ntr) from Escherichia coli. In: Journal of Molecular Biology. 1998 ; Vol. 279, No. 1. pp. 245-255.

Harvard

Bordo, D, Monfort, RLMV, Pijning, T, Kalk, KH, Reizer, J, Saier Jr., MH & Dijkstra, BW 1998, 'The three-dimensional structure of the nitrogen regulatory protein IIA(Ntr) from Escherichia coli', Journal of Molecular Biology, vol. 279, no. 1, pp. 245-255. https://doi.org/10.1006/jmbi.1998.1753

Standard

The three-dimensional structure of the nitrogen regulatory protein IIA(Ntr) from Escherichia coli. / Bordo, Domenico; Monfort, Rob L.M. van; Pijning, Tjaard; Kalk, Kor H.; Reizer, Jonathan; Saier Jr., Milton H.; Dijkstra, Bauke W.

In: Journal of Molecular Biology, Vol. 279, No. 1, 29.05.1998, p. 245-255.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Bordo D, Monfort RLMV, Pijning T, Kalk KH, Reizer J, Saier Jr. MH et al. The three-dimensional structure of the nitrogen regulatory protein IIA(Ntr) from Escherichia coli. Journal of Molecular Biology. 1998 May 29;279(1):245-255. https://doi.org/10.1006/jmbi.1998.1753


BibTeX

@article{46982ea21bbb4e3788bcd83b11214bec,
title = "The three-dimensional structure of the nitrogen regulatory protein IIA(Ntr) from Escherichia coli",
abstract = "The bacterial rpoN operon codes for σ54, which is the key σ factor that, under nitrogen starvation conditions, activates the transcription of genes needed to assimilate ammonia and glutamate. The rpoN operon contains several other open reading frames that are cotranscribed with σ54. The product of one of these, the 17.9 kDa protein IIANtr, is homologous to IIA proteins of the phosphoenolpyruvate:sugar phosphotransferase (PTS) system. IIANtr influences the transcription of σ54-dependent genes through an unknown mechanism and may thereby provide a regulatory link between carbon and nitrogen metabolism. Here we describe the 2.35 {\AA} X-ray structure of Escherichia coli IIANtr. It is the first structure of a IIA enzyme from the fructose-mannitol family of the PTS. The enzyme displays a novel fold characterized by a central mixed parallel/anti-parallel β-sheet surrounded by six α-helices. The active site His73 is situated in a shallow depression on the protein surface.",
keywords = "IIA enzyme, nitrogen metabolism, phosphoenolpyruvate, sugar phosphotransferase system, sigma-54, X-ray structure, PHOSPHOTRANSFERASE SYSTEM, SECONDARY STRUCTURE, BACILLUS-SUBTILIS, IIA-DOMAIN, RPON GENE, PHOSPHOENOLPYRUVATE, METABOLISM, BACTERIA, PHOSPHORYLATION, RESOLUTION",
author = "Domenico Bordo and Monfort, {Rob L.M. van} and Tjaard Pijning and Kalk, {Kor H.} and Jonathan Reizer and {Saier Jr.}, {Milton H.} and Dijkstra, {Bauke W.}",
note = "Relation: https://www.rug.nl/gbb/ date_submitted:2009 Rights: University of Groningen, Groningen Biomolecular Sciences and Biotechnology Institute",
year = "1998",
month = may,
day = "29",
doi = "10.1006/jmbi.1998.1753",
language = "English",
volume = "279",
pages = "245--255",
journal = "Journal of Molecular Biology",
issn = "0022-2836",
publisher = "Academic Press",
number = "1",

}

RIS

TY - JOUR

T1 - The three-dimensional structure of the nitrogen regulatory protein IIA(Ntr) from Escherichia coli

AU - Bordo, Domenico

AU - Monfort, Rob L.M. van

AU - Pijning, Tjaard

AU - Kalk, Kor H.

AU - Reizer, Jonathan

AU - Saier Jr., Milton H.

AU - Dijkstra, Bauke W.

N1 - Relation: https://www.rug.nl/gbb/ date_submitted:2009 Rights: University of Groningen, Groningen Biomolecular Sciences and Biotechnology Institute

PY - 1998/5/29

Y1 - 1998/5/29

N2 - The bacterial rpoN operon codes for σ54, which is the key σ factor that, under nitrogen starvation conditions, activates the transcription of genes needed to assimilate ammonia and glutamate. The rpoN operon contains several other open reading frames that are cotranscribed with σ54. The product of one of these, the 17.9 kDa protein IIANtr, is homologous to IIA proteins of the phosphoenolpyruvate:sugar phosphotransferase (PTS) system. IIANtr influences the transcription of σ54-dependent genes through an unknown mechanism and may thereby provide a regulatory link between carbon and nitrogen metabolism. Here we describe the 2.35 Å X-ray structure of Escherichia coli IIANtr. It is the first structure of a IIA enzyme from the fructose-mannitol family of the PTS. The enzyme displays a novel fold characterized by a central mixed parallel/anti-parallel β-sheet surrounded by six α-helices. The active site His73 is situated in a shallow depression on the protein surface.

AB - The bacterial rpoN operon codes for σ54, which is the key σ factor that, under nitrogen starvation conditions, activates the transcription of genes needed to assimilate ammonia and glutamate. The rpoN operon contains several other open reading frames that are cotranscribed with σ54. The product of one of these, the 17.9 kDa protein IIANtr, is homologous to IIA proteins of the phosphoenolpyruvate:sugar phosphotransferase (PTS) system. IIANtr influences the transcription of σ54-dependent genes through an unknown mechanism and may thereby provide a regulatory link between carbon and nitrogen metabolism. Here we describe the 2.35 Å X-ray structure of Escherichia coli IIANtr. It is the first structure of a IIA enzyme from the fructose-mannitol family of the PTS. The enzyme displays a novel fold characterized by a central mixed parallel/anti-parallel β-sheet surrounded by six α-helices. The active site His73 is situated in a shallow depression on the protein surface.

KW - IIA enzyme

KW - nitrogen metabolism

KW - phosphoenolpyruvate

KW - sugar phosphotransferase system

KW - sigma-54

KW - X-ray structure

KW - PHOSPHOTRANSFERASE SYSTEM

KW - SECONDARY STRUCTURE

KW - BACILLUS-SUBTILIS

KW - IIA-DOMAIN

KW - RPON GENE

KW - PHOSPHOENOLPYRUVATE

KW - METABOLISM

KW - BACTERIA

KW - PHOSPHORYLATION

KW - RESOLUTION

U2 - 10.1006/jmbi.1998.1753

DO - 10.1006/jmbi.1998.1753

M3 - Article

VL - 279

SP - 245

EP - 255

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

SN - 0022-2836

IS - 1

ER -

ID: 3726729