Eintrag weiter verarbeiten
The 3.7 Å projection map of the glycerol facilitator GlpF: a variant of the aquaporin tetramer
Gespeichert in:
Zeitschriftentitel: | EMBO reports |
---|---|
Personen und Körperschaften: | , , , , , , , |
In: | EMBO reports, 1, 2000, 2, S. 183-189 |
Format: | E-Article |
Sprache: | Englisch |
veröffentlicht: |
Springer Science and Business Media LLC
|
Schlagwörter: |
author_facet |
Braun, Thomas Philippsen, Ansgar Wirtz, Sabine Borgnia, Mario J. Agre, Peter Kühlbrandt, Werner Engel, Andreas Stahlberg, Henning Braun, Thomas Philippsen, Ansgar Wirtz, Sabine Borgnia, Mario J. Agre, Peter Kühlbrandt, Werner Engel, Andreas Stahlberg, Henning |
---|---|
author |
Braun, Thomas Philippsen, Ansgar Wirtz, Sabine Borgnia, Mario J. Agre, Peter Kühlbrandt, Werner Engel, Andreas Stahlberg, Henning |
spellingShingle |
Braun, Thomas Philippsen, Ansgar Wirtz, Sabine Borgnia, Mario J. Agre, Peter Kühlbrandt, Werner Engel, Andreas Stahlberg, Henning EMBO reports The 3.7 Å projection map of the glycerol facilitator GlpF: a variant of the aquaporin tetramer Genetics Molecular Biology Biochemistry |
author_sort |
braun, thomas |
spelling |
Braun, Thomas Philippsen, Ansgar Wirtz, Sabine Borgnia, Mario J. Agre, Peter Kühlbrandt, Werner Engel, Andreas Stahlberg, Henning 1469-221X 1469-3178 Springer Science and Business Media LLC Genetics Molecular Biology Biochemistry http://dx.doi.org/10.1093/embo-reports/kvd022 <jats:p>GlpF, the glycerol facilitator protein of <jats:italic>Escherichia coli</jats:italic>, is an archetypal member of the aquaporin superfamily. To assess its structure, recombinant histidine‐tagged protein was overexpressed, solubilized in octylglucoside and purified to homogeneity. Negative stain electron microscopy of solubilized GlpF protein revealed a tetrameric structure of ∼80 Å side length. Scanning transmission electron microscopy yielded a mass of 170 kDa, corroborating the tetrameric nature of GlpF. Reconstitution of GlpF in the presence of lipids produced highly ordered two‐dimensional crystals, which diffracted electrons to 3.6 Å resolution. Cryoelectron microscopy provided a 3.7 Å projection map exhibiting a unit cell comprised of two tetramers. In projection, GlpF is similar to AQP1, the erythrocyte water channel. However, the major density minimum within each monomer is distinctly larger in GlpF than in AQP1.</jats:p> The 3.7 Å projection map of the glycerol facilitator GlpF: a variant of the aquaporin tetramer EMBO reports |
doi_str_mv |
10.1093/embo-reports/kvd022 |
facet_avail |
Online Free |
finc_class_facet |
Biologie Chemie und Pharmazie |
format |
ElectronicArticle |
fullrecord |
blob:ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTA5My9lbWJvLXJlcG9ydHMva3ZkMDIy |
id |
ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTA5My9lbWJvLXJlcG9ydHMva3ZkMDIy |
institution |
DE-Zi4 DE-Gla1 DE-15 DE-Pl11 DE-Rs1 DE-14 DE-105 DE-Ch1 DE-L229 DE-D275 DE-Bn3 DE-Brt1 DE-Zwi2 DE-D161 |
imprint |
Springer Science and Business Media LLC, 2000 |
imprint_str_mv |
Springer Science and Business Media LLC, 2000 |
issn |
1469-221X 1469-3178 |
issn_str_mv |
1469-221X 1469-3178 |
language |
English |
mega_collection |
Springer Science and Business Media LLC (CrossRef) |
match_str |
braun2000the37aprojectionmapoftheglycerolfacilitatorglpfavariantoftheaquaporintetramer |
publishDateSort |
2000 |
publisher |
Springer Science and Business Media LLC |
recordtype |
ai |
record_format |
ai |
series |
EMBO reports |
source_id |
49 |
title |
The 3.7 Å projection map of the glycerol facilitator GlpF: a variant of the aquaporin tetramer |
title_unstemmed |
The 3.7 Å projection map of the glycerol facilitator GlpF: a variant of the aquaporin tetramer |
title_full |
The 3.7 Å projection map of the glycerol facilitator GlpF: a variant of the aquaporin tetramer |
title_fullStr |
The 3.7 Å projection map of the glycerol facilitator GlpF: a variant of the aquaporin tetramer |
title_full_unstemmed |
The 3.7 Å projection map of the glycerol facilitator GlpF: a variant of the aquaporin tetramer |
title_short |
The 3.7 Å projection map of the glycerol facilitator GlpF: a variant of the aquaporin tetramer |
title_sort |
the 3.7 å projection map of the glycerol facilitator glpf: a variant of the aquaporin tetramer |
topic |
Genetics Molecular Biology Biochemistry |
url |
http://dx.doi.org/10.1093/embo-reports/kvd022 |
publishDate |
2000 |
physical |
183-189 |
description |
<jats:p>GlpF, the glycerol facilitator protein of <jats:italic>Escherichia coli</jats:italic>, is an archetypal member of the aquaporin superfamily. To assess its structure, recombinant histidine‐tagged protein was overexpressed, solubilized in octylglucoside and purified to homogeneity. Negative stain electron microscopy of solubilized GlpF protein revealed a tetrameric structure of ∼80 Å side length. Scanning transmission electron microscopy yielded a mass of 170 kDa, corroborating the tetrameric nature of GlpF. Reconstitution of GlpF in the presence of lipids produced highly ordered two‐dimensional crystals, which diffracted electrons to 3.6 Å resolution. Cryoelectron microscopy provided a 3.7 Å projection map exhibiting a unit cell comprised of two tetramers. In projection, GlpF is similar to AQP1, the erythrocyte water channel. However, the major density minimum within each monomer is distinctly larger in GlpF than in AQP1.</jats:p> |
container_issue |
2 |
container_start_page |
183 |
container_title |
EMBO reports |
container_volume |
1 |
format_de105 |
Article, E-Article |
format_de14 |
Article, E-Article |
format_de15 |
Article, E-Article |
format_de520 |
Article, E-Article |
format_de540 |
Article, E-Article |
format_dech1 |
Article, E-Article |
format_ded117 |
Article, E-Article |
format_degla1 |
E-Article |
format_del152 |
Buch |
format_del189 |
Article, E-Article |
format_dezi4 |
Article |
format_dezwi2 |
Article, E-Article |
format_finc |
Article, E-Article |
format_nrw |
Article, E-Article |
_version_ |
1792342391411179522 |
geogr_code |
not assigned |
last_indexed |
2024-03-01T16:35:03.987Z |
geogr_code_person |
not assigned |
openURL |
url_ver=Z39.88-2004&ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fvufind.svn.sourceforge.net%3Agenerator&rft.title=The+3.7+%C3%85+projection+map+of+the+glycerol+facilitator+GlpF%3A+a+variant+of+the+aquaporin+tetramer&rft.date=2000-08-01&genre=article&issn=1469-3178&volume=1&issue=2&spage=183&epage=189&pages=183-189&jtitle=EMBO+reports&atitle=The+3.7+%C3%85+projection+map+of+the+glycerol+facilitator+GlpF%3A+a+variant+of+the+aquaporin+tetramer&aulast=Stahlberg&aufirst=Henning&rft_id=info%3Adoi%2F10.1093%2Fembo-reports%2Fkvd022&rft.language%5B0%5D=eng |
SOLR | |
_version_ | 1792342391411179522 |
author | Braun, Thomas, Philippsen, Ansgar, Wirtz, Sabine, Borgnia, Mario J., Agre, Peter, Kühlbrandt, Werner, Engel, Andreas, Stahlberg, Henning |
author_facet | Braun, Thomas, Philippsen, Ansgar, Wirtz, Sabine, Borgnia, Mario J., Agre, Peter, Kühlbrandt, Werner, Engel, Andreas, Stahlberg, Henning, Braun, Thomas, Philippsen, Ansgar, Wirtz, Sabine, Borgnia, Mario J., Agre, Peter, Kühlbrandt, Werner, Engel, Andreas, Stahlberg, Henning |
author_sort | braun, thomas |
container_issue | 2 |
container_start_page | 183 |
container_title | EMBO reports |
container_volume | 1 |
description | <jats:p>GlpF, the glycerol facilitator protein of <jats:italic>Escherichia coli</jats:italic>, is an archetypal member of the aquaporin superfamily. To assess its structure, recombinant histidine‐tagged protein was overexpressed, solubilized in octylglucoside and purified to homogeneity. Negative stain electron microscopy of solubilized GlpF protein revealed a tetrameric structure of ∼80 Å side length. Scanning transmission electron microscopy yielded a mass of 170 kDa, corroborating the tetrameric nature of GlpF. Reconstitution of GlpF in the presence of lipids produced highly ordered two‐dimensional crystals, which diffracted electrons to 3.6 Å resolution. Cryoelectron microscopy provided a 3.7 Å projection map exhibiting a unit cell comprised of two tetramers. In projection, GlpF is similar to AQP1, the erythrocyte water channel. However, the major density minimum within each monomer is distinctly larger in GlpF than in AQP1.</jats:p> |
doi_str_mv | 10.1093/embo-reports/kvd022 |
facet_avail | Online, Free |
finc_class_facet | Biologie, Chemie und Pharmazie |
format | ElectronicArticle |
format_de105 | Article, E-Article |
format_de14 | Article, E-Article |
format_de15 | Article, E-Article |
format_de520 | Article, E-Article |
format_de540 | Article, E-Article |
format_dech1 | Article, E-Article |
format_ded117 | Article, E-Article |
format_degla1 | E-Article |
format_del152 | Buch |
format_del189 | Article, E-Article |
format_dezi4 | Article |
format_dezwi2 | Article, E-Article |
format_finc | Article, E-Article |
format_nrw | Article, E-Article |
geogr_code | not assigned |
geogr_code_person | not assigned |
id | ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTA5My9lbWJvLXJlcG9ydHMva3ZkMDIy |
imprint | Springer Science and Business Media LLC, 2000 |
imprint_str_mv | Springer Science and Business Media LLC, 2000 |
institution | DE-Zi4, DE-Gla1, DE-15, DE-Pl11, DE-Rs1, DE-14, DE-105, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161 |
issn | 1469-221X, 1469-3178 |
issn_str_mv | 1469-221X, 1469-3178 |
language | English |
last_indexed | 2024-03-01T16:35:03.987Z |
match_str | braun2000the37aprojectionmapoftheglycerolfacilitatorglpfavariantoftheaquaporintetramer |
mega_collection | Springer Science and Business Media LLC (CrossRef) |
physical | 183-189 |
publishDate | 2000 |
publishDateSort | 2000 |
publisher | Springer Science and Business Media LLC |
record_format | ai |
recordtype | ai |
series | EMBO reports |
source_id | 49 |
spelling | Braun, Thomas Philippsen, Ansgar Wirtz, Sabine Borgnia, Mario J. Agre, Peter Kühlbrandt, Werner Engel, Andreas Stahlberg, Henning 1469-221X 1469-3178 Springer Science and Business Media LLC Genetics Molecular Biology Biochemistry http://dx.doi.org/10.1093/embo-reports/kvd022 <jats:p>GlpF, the glycerol facilitator protein of <jats:italic>Escherichia coli</jats:italic>, is an archetypal member of the aquaporin superfamily. To assess its structure, recombinant histidine‐tagged protein was overexpressed, solubilized in octylglucoside and purified to homogeneity. Negative stain electron microscopy of solubilized GlpF protein revealed a tetrameric structure of ∼80 Å side length. Scanning transmission electron microscopy yielded a mass of 170 kDa, corroborating the tetrameric nature of GlpF. Reconstitution of GlpF in the presence of lipids produced highly ordered two‐dimensional crystals, which diffracted electrons to 3.6 Å resolution. Cryoelectron microscopy provided a 3.7 Å projection map exhibiting a unit cell comprised of two tetramers. In projection, GlpF is similar to AQP1, the erythrocyte water channel. However, the major density minimum within each monomer is distinctly larger in GlpF than in AQP1.</jats:p> The 3.7 Å projection map of the glycerol facilitator GlpF: a variant of the aquaporin tetramer EMBO reports |
spellingShingle | Braun, Thomas, Philippsen, Ansgar, Wirtz, Sabine, Borgnia, Mario J., Agre, Peter, Kühlbrandt, Werner, Engel, Andreas, Stahlberg, Henning, EMBO reports, The 3.7 Å projection map of the glycerol facilitator GlpF: a variant of the aquaporin tetramer, Genetics, Molecular Biology, Biochemistry |
title | The 3.7 Å projection map of the glycerol facilitator GlpF: a variant of the aquaporin tetramer |
title_full | The 3.7 Å projection map of the glycerol facilitator GlpF: a variant of the aquaporin tetramer |
title_fullStr | The 3.7 Å projection map of the glycerol facilitator GlpF: a variant of the aquaporin tetramer |
title_full_unstemmed | The 3.7 Å projection map of the glycerol facilitator GlpF: a variant of the aquaporin tetramer |
title_short | The 3.7 Å projection map of the glycerol facilitator GlpF: a variant of the aquaporin tetramer |
title_sort | the 3.7 å projection map of the glycerol facilitator glpf: a variant of the aquaporin tetramer |
title_unstemmed | The 3.7 Å projection map of the glycerol facilitator GlpF: a variant of the aquaporin tetramer |
topic | Genetics, Molecular Biology, Biochemistry |
url | http://dx.doi.org/10.1093/embo-reports/kvd022 |