Solution nuclear magnetic resonance structure of membrane-integral diacylglycerol kinase

Wade Van Horn, Hak Jun Kim, Charles D. Ellis, Arina Hadziselimovic, Endah S. Sulistijo, Murthy D. Karra, Changlin Tian, Frank D. Sönnichsen, Charles R. Sanders

Research output: Contribution to journalArticle

166 Citations (Scopus)

Abstract

Escherichia coli diacylglycerol kinase (DAGK) represents a family of integral membrane enzymes that is unrelated to all other phosphotransferases. We have determined the three-dimensional structure of the DAGK homotrimer with the use of solution nuclear magnetic resonance. The third transmembrane helix from each subunit is domain-swapped with the first and second transmembrane segments from an adjacent subunit. Each of DAGK's three active sites resembles a portico. The cornice of the portico appears to be the determinant of DAGK's lipid substrate specificity and overhangs the site of phosphoryl transfer near the water-membrane interface. Mutations to cysteine that caused severe misfolding were located in or near the active site, indicating a high degree of overlap between sites responsible for folding and for catalysis.

Original languageEnglish (US)
Pages (from-to)1726-1729
Number of pages4
JournalScience
Volume324
Issue number5935
DOIs
StatePublished - Jun 26 2009
Externally publishedYes

Fingerprint

Diacylglycerol Kinase
Catalytic Domain
Magnetic Resonance Spectroscopy
Membranes
Substrate Specificity
Catalysis
Cysteine
Phosphotransferases
Escherichia coli
Lipids
Mutation
Water
Enzymes

ASJC Scopus subject areas

  • General
  • Medicine(all)

Cite this

Van Horn, W., Kim, H. J., Ellis, C. D., Hadziselimovic, A., Sulistijo, E. S., Karra, M. D., ... Sanders, C. R. (2009). Solution nuclear magnetic resonance structure of membrane-integral diacylglycerol kinase. Science, 324(5935), 1726-1729. https://doi.org/10.1126/science.1171716

Solution nuclear magnetic resonance structure of membrane-integral diacylglycerol kinase. / Van Horn, Wade; Kim, Hak Jun; Ellis, Charles D.; Hadziselimovic, Arina; Sulistijo, Endah S.; Karra, Murthy D.; Tian, Changlin; Sönnichsen, Frank D.; Sanders, Charles R.

In: Science, Vol. 324, No. 5935, 26.06.2009, p. 1726-1729.

Research output: Contribution to journalArticle

Van Horn, W, Kim, HJ, Ellis, CD, Hadziselimovic, A, Sulistijo, ES, Karra, MD, Tian, C, Sönnichsen, FD & Sanders, CR 2009, 'Solution nuclear magnetic resonance structure of membrane-integral diacylglycerol kinase', Science, vol. 324, no. 5935, pp. 1726-1729. https://doi.org/10.1126/science.1171716
Van Horn W, Kim HJ, Ellis CD, Hadziselimovic A, Sulistijo ES, Karra MD et al. Solution nuclear magnetic resonance structure of membrane-integral diacylglycerol kinase. Science. 2009 Jun 26;324(5935):1726-1729. https://doi.org/10.1126/science.1171716
Van Horn, Wade ; Kim, Hak Jun ; Ellis, Charles D. ; Hadziselimovic, Arina ; Sulistijo, Endah S. ; Karra, Murthy D. ; Tian, Changlin ; Sönnichsen, Frank D. ; Sanders, Charles R. / Solution nuclear magnetic resonance structure of membrane-integral diacylglycerol kinase. In: Science. 2009 ; Vol. 324, No. 5935. pp. 1726-1729.
@article{3a3111d52775480b96f7851729ae6b27,
title = "Solution nuclear magnetic resonance structure of membrane-integral diacylglycerol kinase",
abstract = "Escherichia coli diacylglycerol kinase (DAGK) represents a family of integral membrane enzymes that is unrelated to all other phosphotransferases. We have determined the three-dimensional structure of the DAGK homotrimer with the use of solution nuclear magnetic resonance. The third transmembrane helix from each subunit is domain-swapped with the first and second transmembrane segments from an adjacent subunit. Each of DAGK's three active sites resembles a portico. The cornice of the portico appears to be the determinant of DAGK's lipid substrate specificity and overhangs the site of phosphoryl transfer near the water-membrane interface. Mutations to cysteine that caused severe misfolding were located in or near the active site, indicating a high degree of overlap between sites responsible for folding and for catalysis.",
author = "{Van Horn}, Wade and Kim, {Hak Jun} and Ellis, {Charles D.} and Arina Hadziselimovic and Sulistijo, {Endah S.} and Karra, {Murthy D.} and Changlin Tian and S{\"o}nnichsen, {Frank D.} and Sanders, {Charles R.}",
year = "2009",
month = "6",
day = "26",
doi = "10.1126/science.1171716",
language = "English (US)",
volume = "324",
pages = "1726--1729",
journal = "Science",
issn = "0036-8075",
publisher = "American Association for the Advancement of Science",
number = "5935",

}

TY - JOUR

T1 - Solution nuclear magnetic resonance structure of membrane-integral diacylglycerol kinase

AU - Van Horn, Wade

AU - Kim, Hak Jun

AU - Ellis, Charles D.

AU - Hadziselimovic, Arina

AU - Sulistijo, Endah S.

AU - Karra, Murthy D.

AU - Tian, Changlin

AU - Sönnichsen, Frank D.

AU - Sanders, Charles R.

PY - 2009/6/26

Y1 - 2009/6/26

N2 - Escherichia coli diacylglycerol kinase (DAGK) represents a family of integral membrane enzymes that is unrelated to all other phosphotransferases. We have determined the three-dimensional structure of the DAGK homotrimer with the use of solution nuclear magnetic resonance. The third transmembrane helix from each subunit is domain-swapped with the first and second transmembrane segments from an adjacent subunit. Each of DAGK's three active sites resembles a portico. The cornice of the portico appears to be the determinant of DAGK's lipid substrate specificity and overhangs the site of phosphoryl transfer near the water-membrane interface. Mutations to cysteine that caused severe misfolding were located in or near the active site, indicating a high degree of overlap between sites responsible for folding and for catalysis.

AB - Escherichia coli diacylglycerol kinase (DAGK) represents a family of integral membrane enzymes that is unrelated to all other phosphotransferases. We have determined the three-dimensional structure of the DAGK homotrimer with the use of solution nuclear magnetic resonance. The third transmembrane helix from each subunit is domain-swapped with the first and second transmembrane segments from an adjacent subunit. Each of DAGK's three active sites resembles a portico. The cornice of the portico appears to be the determinant of DAGK's lipid substrate specificity and overhangs the site of phosphoryl transfer near the water-membrane interface. Mutations to cysteine that caused severe misfolding were located in or near the active site, indicating a high degree of overlap between sites responsible for folding and for catalysis.

UR - http://www.scopus.com/inward/record.url?scp=67649908268&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=67649908268&partnerID=8YFLogxK

U2 - 10.1126/science.1171716

DO - 10.1126/science.1171716

M3 - Article

C2 - 19556511

AN - SCOPUS:67649908268

VL - 324

SP - 1726

EP - 1729

JO - Science

JF - Science

SN - 0036-8075

IS - 5935

ER -