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Solution Nuclear Magnetic Resonance Structure of Membrane-Integral Diacylglycerol Kinase

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 he... Full description

Journal Title: Science (Washington) 26 June 2009, Vol.324(5935), pp.1726-1729
Main Author: Van Horn, Wade
Other Authors: Kim, Hak-Jun , Ellis, Charles , Hadziselimovic, Arina , Sulistijo, Endah , Karra, Murthy , Tian, Changlin , Soennichsen, Frank , Sanders, Charles
Format: Electronic Article Electronic Article
Language: English
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ID: ISSN: 0036-8075
Link: http://search.proquest.com/docview/36229744/
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title: Solution Nuclear Magnetic Resonance Structure of Membrane-Integral Diacylglycerol Kinase
format: Article
creator:
  • Van Horn, Wade
  • Kim, Hak-Jun
  • Ellis, Charles
  • Hadziselimovic, Arina
  • Sulistijo, Endah
  • Karra, Murthy
  • Tian, Changlin
  • Soennichsen, Frank
  • Sanders, Charles
subjects:
  • Kinases
  • Nuclear Magnetic Resonance
  • Lipids
  • Escherichia Coli
  • Overhang
  • Carbon Monoxide
  • Segments
  • Mutations
  • Miscellaneous Sciences (So)
  • Article
ispartof: Science (Washington), 26 June 2009, Vol.324(5935), pp.1726-1729
description: 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. [PUBLICATION ]
language: eng
source:
identifier: ISSN: 0036-8075
fulltext: no_fulltext
issn:
  • 00368075
  • 0036-8075
url: Link


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titleSolution Nuclear Magnetic Resonance Structure of Membrane-Integral Diacylglycerol Kinase
creatorVan Horn, Wade ; Kim, Hak-Jun ; Ellis, Charles ; Hadziselimovic, Arina ; Sulistijo, Endah ; Karra, Murthy ; Tian, Changlin ; Soennichsen, Frank ; Sanders, Charles
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ispartofScience (Washington), 26 June 2009, Vol.324(5935), pp.1726-1729
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subjectKinases ; Nuclear Magnetic Resonance ; Lipids ; Escherichia Coli ; Overhang ; Carbon Monoxide ; Segments ; Mutations ; Miscellaneous Sciences (So) ; Article
descriptionEscherichia 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. [PUBLICATION ]
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titleSolution Nuclear Magnetic Resonance Structure of Membrane-Integral Diacylglycerol Kinase
descriptionEscherichia 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. [PUBLICATION ]
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titleSolution Nuclear Magnetic Resonance Structure of Membrane-Integral Diacylglycerol Kinase
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abstractEscherichia 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. [PUBLICATION ABSTRACT]
urlhttp://search.proquest.com/docview/36229744/
doi10.1126/science.1171716
eissn10959203
date2009-06-26