Publication

The structure of an energy-coupling protein from bacteria, IIBcellobiose, reveals similarity to eukaryotic protein tyrosine phosphatases

van Montfort, R. L. M., Pijning, T., Kalk, K. H., Reizer, J., Saier Jr., M. H., Thunnissen, M. M. G. M., Robillard, G. T. & Dijkstra, B. W., 15-Feb-1997, In : Structure. 5, 2, p. 217-225 9 p.

Research output: Contribution to journalArticleAcademic

APA

van Montfort, R. L. M., Pijning, T., Kalk, K. H., Reizer, J., Saier Jr., M. H., Thunnissen, M. M. G. M., Robillard, G. T., & Dijkstra, B. W. (1997). The structure of an energy-coupling protein from bacteria, IIBcellobiose, reveals similarity to eukaryotic protein tyrosine phosphatases. Structure, 5(2), 217-225. https://doi.org/10.1016/S0969-2126(97)00180-9

Author

van Montfort, Rob L.M. ; Pijning, Tjaard ; Kalk, Kor H. ; Reizer, Jonathan ; Saier Jr., Milton H. ; Thunnissen, Marjolein M.G.M. ; Robillard, George T. ; Dijkstra, Bauke W. / The structure of an energy-coupling protein from bacteria, IIBcellobiose, reveals similarity to eukaryotic protein tyrosine phosphatases. In: Structure. 1997 ; Vol. 5, No. 2. pp. 217-225.

Harvard

van Montfort, RLM, Pijning, T, Kalk, KH, Reizer, J, Saier Jr., MH, Thunnissen, MMGM, Robillard, GT & Dijkstra, BW 1997, 'The structure of an energy-coupling protein from bacteria, IIBcellobiose, reveals similarity to eukaryotic protein tyrosine phosphatases', Structure, vol. 5, no. 2, pp. 217-225. https://doi.org/10.1016/S0969-2126(97)00180-9

Standard

The structure of an energy-coupling protein from bacteria, IIBcellobiose, reveals similarity to eukaryotic protein tyrosine phosphatases. / van Montfort, Rob L.M.; Pijning, Tjaard; Kalk, Kor H.; Reizer, Jonathan; Saier Jr., Milton H.; Thunnissen, Marjolein M.G.M.; Robillard, George T.; Dijkstra, Bauke W.

In: Structure, Vol. 5, No. 2, 15.02.1997, p. 217-225.

Research output: Contribution to journalArticleAcademic

Vancouver

van Montfort RLM, Pijning T, Kalk KH, Reizer J, Saier Jr. MH, Thunnissen MMGM et al. The structure of an energy-coupling protein from bacteria, IIBcellobiose, reveals similarity to eukaryotic protein tyrosine phosphatases. Structure. 1997 Feb 15;5(2):217-225. https://doi.org/10.1016/S0969-2126(97)00180-9


BibTeX

@article{f9fc47d946654897a444c23d4bccfcd2,
title = "The structure of an energy-coupling protein from bacteria, IIBcellobiose, reveals similarity to eukaryotic protein tyrosine phosphatases",
abstract = "Background: The bacterial phosphoenolpyruvate-dependent phosphotransferase system (PTS) mediates the energy-driven uptake of carbohydrates and their concomitant phosphorylation, In addition, the PTS is intimately involved in the regulation of a variety of metabolic and transcriptional processes in the bacterium. The multiprotein PTS consists of a membrane channel and at least four cytoplasmic proteins or protein domains that sequentially transfer a phosphoryl group from phosphoenolpyruvate to the transported carbohydrate, Determination of the three-dimensional structure of the IIB enzymes within the multiprotein complex would provide insights into the mechanisms by which they promote efficient transport by the membrane channel IIC protein and phosphorylate the transported carbohydrate on the inside of the cell,Results: The crystal structure of the IIB enzyme specific for cellobiose, IIBcellobiose (molecular weight 11.4 kDa), has been determined to a resolution of 1.8 Angstrom and refined to an R factor of 18.7% (R(free) of 24.1%). The enzyme consists of a single four-stranded parallel beta sheet flanked by helices on both sides. The phosphorylation site (Cys10) is located at the C-terminal end of the first beta strand, No positively charged residues, which could assist in phosphoryl-transfer, can be found in or near the active site. The fold of IIBcellobiose is remarkably similar to that of the mammalian low molecular weight protein tyrosine phosphatases.Conclusions: A comparison between IIBcellobiose and the structurally similar low molecular weight protein tyrosine phosphatases provides insight into the mechanism of the phosphoryltransfer reactions in which IIBcellobiose is involved, The differences in tertiary structure and active-site composition between IIBcellobiose and the glucose-specific IIBglucose give a structural explanation why the carbohydrate-specific components of different families cannot complement each other.",
keywords = "carbohydrate transport, cysteine phosphorylation, IIB enzymes, PTS, X-ray structure, 3-DIMENSIONAL NMR-SPECTROSCOPY, ESCHERICHIA-COLI, PHOSPHOTRANSFERASE SYSTEM, STAPHYLOCOCCUS-AUREUS, NUCLEOTIDE-SEQUENCE, CATALYTIC MECHANISM, BACILLUS-SUBTILIS, GLUCOSE PERMEASE, IIA-DOMAIN, ENZYME-II",
author = "{van Montfort}, {Rob L.M.} and Tjaard Pijning and Kalk, {Kor H.} and Jonathan Reizer and {Saier Jr.}, {Milton H.} and Thunnissen, {Marjolein M.G.M.} and Robillard, {George T.} 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 = "1997",
month = feb,
day = "15",
doi = "10.1016/S0969-2126(97)00180-9",
language = "English",
volume = "5",
pages = "217--225",
journal = "Structure",
issn = "1878-4186",
publisher = "CELL PRESS",
number = "2",

}

RIS

TY - JOUR

T1 - The structure of an energy-coupling protein from bacteria, IIBcellobiose, reveals similarity to eukaryotic protein tyrosine phosphatases

AU - van Montfort, Rob L.M.

AU - Pijning, Tjaard

AU - Kalk, Kor H.

AU - Reizer, Jonathan

AU - Saier Jr., Milton H.

AU - Thunnissen, Marjolein M.G.M.

AU - Robillard, George T.

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 - 1997/2/15

Y1 - 1997/2/15

N2 - Background: The bacterial phosphoenolpyruvate-dependent phosphotransferase system (PTS) mediates the energy-driven uptake of carbohydrates and their concomitant phosphorylation, In addition, the PTS is intimately involved in the regulation of a variety of metabolic and transcriptional processes in the bacterium. The multiprotein PTS consists of a membrane channel and at least four cytoplasmic proteins or protein domains that sequentially transfer a phosphoryl group from phosphoenolpyruvate to the transported carbohydrate, Determination of the three-dimensional structure of the IIB enzymes within the multiprotein complex would provide insights into the mechanisms by which they promote efficient transport by the membrane channel IIC protein and phosphorylate the transported carbohydrate on the inside of the cell,Results: The crystal structure of the IIB enzyme specific for cellobiose, IIBcellobiose (molecular weight 11.4 kDa), has been determined to a resolution of 1.8 Angstrom and refined to an R factor of 18.7% (R(free) of 24.1%). The enzyme consists of a single four-stranded parallel beta sheet flanked by helices on both sides. The phosphorylation site (Cys10) is located at the C-terminal end of the first beta strand, No positively charged residues, which could assist in phosphoryl-transfer, can be found in or near the active site. The fold of IIBcellobiose is remarkably similar to that of the mammalian low molecular weight protein tyrosine phosphatases.Conclusions: A comparison between IIBcellobiose and the structurally similar low molecular weight protein tyrosine phosphatases provides insight into the mechanism of the phosphoryltransfer reactions in which IIBcellobiose is involved, The differences in tertiary structure and active-site composition between IIBcellobiose and the glucose-specific IIBglucose give a structural explanation why the carbohydrate-specific components of different families cannot complement each other.

AB - Background: The bacterial phosphoenolpyruvate-dependent phosphotransferase system (PTS) mediates the energy-driven uptake of carbohydrates and their concomitant phosphorylation, In addition, the PTS is intimately involved in the regulation of a variety of metabolic and transcriptional processes in the bacterium. The multiprotein PTS consists of a membrane channel and at least four cytoplasmic proteins or protein domains that sequentially transfer a phosphoryl group from phosphoenolpyruvate to the transported carbohydrate, Determination of the three-dimensional structure of the IIB enzymes within the multiprotein complex would provide insights into the mechanisms by which they promote efficient transport by the membrane channel IIC protein and phosphorylate the transported carbohydrate on the inside of the cell,Results: The crystal structure of the IIB enzyme specific for cellobiose, IIBcellobiose (molecular weight 11.4 kDa), has been determined to a resolution of 1.8 Angstrom and refined to an R factor of 18.7% (R(free) of 24.1%). The enzyme consists of a single four-stranded parallel beta sheet flanked by helices on both sides. The phosphorylation site (Cys10) is located at the C-terminal end of the first beta strand, No positively charged residues, which could assist in phosphoryl-transfer, can be found in or near the active site. The fold of IIBcellobiose is remarkably similar to that of the mammalian low molecular weight protein tyrosine phosphatases.Conclusions: A comparison between IIBcellobiose and the structurally similar low molecular weight protein tyrosine phosphatases provides insight into the mechanism of the phosphoryltransfer reactions in which IIBcellobiose is involved, The differences in tertiary structure and active-site composition between IIBcellobiose and the glucose-specific IIBglucose give a structural explanation why the carbohydrate-specific components of different families cannot complement each other.

KW - carbohydrate transport

KW - cysteine phosphorylation

KW - IIB enzymes

KW - PTS

KW - X-ray structure

KW - 3-DIMENSIONAL NMR-SPECTROSCOPY

KW - ESCHERICHIA-COLI

KW - PHOSPHOTRANSFERASE SYSTEM

KW - STAPHYLOCOCCUS-AUREUS

KW - NUCLEOTIDE-SEQUENCE

KW - CATALYTIC MECHANISM

KW - BACILLUS-SUBTILIS

KW - GLUCOSE PERMEASE

KW - IIA-DOMAIN

KW - ENZYME-II

U2 - 10.1016/S0969-2126(97)00180-9

DO - 10.1016/S0969-2126(97)00180-9

M3 - Article

VL - 5

SP - 217

EP - 225

JO - Structure

JF - Structure

SN - 1878-4186

IS - 2

ER -

ID: 1212199