- EMDB-5202: Influence of the cytoplasmic domains of aquaporin-4 on water cond... -
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Basic information
Entry
Database: EMDB / ID: EMD-5202
Title
Influence of the cytoplasmic domains of aquaporin-4 on water conduction and array formation.
Map data
This is an image of a surface rendered of Aquaporin-4
Sample
Sample: rat aquaporin-4 S180D mutant
Protein or peptide: aquaporin-4
Keywords
Water channel / Aquaporin / Cell adhesion
Function / homology
Function and homology information
Passive transport by Aquaporins / cerebrospinal fluid secretion / renal water absorption / regulation of vascular endothelial growth factor production / cerebrospinal fluid circulation / astrocyte end-foot / intracellular water homeostasis / water transport / water channel activity / negative regulation of cell adhesion molecule production ...Passive transport by Aquaporins / cerebrospinal fluid secretion / renal water absorption / regulation of vascular endothelial growth factor production / cerebrospinal fluid circulation / astrocyte end-foot / intracellular water homeostasis / water transport / water channel activity / negative regulation of cell adhesion molecule production / cell projection membrane / multicellular organismal-level water homeostasis / Vasopressin regulates renal water homeostasis via Aquaporins / cellular response to interleukin-6 / negative regulation of interleukin-1 beta production / negative regulation of interleukin-6 production / cellular response to interleukin-1 / response to glucocorticoid / T-tubule / basal plasma membrane / establishment of localization in cell / cellular response to estradiol stimulus / female pregnancy / cellular response to glucose stimulus / sensory perception of sound / carbon dioxide transport / sarcolemma / cellular response to type II interferon / cell-cell adhesion / cell-cell junction / basolateral plasma membrane / protein homotetramerization / endosome membrane / external side of plasma membrane / protein-containing complex / extracellular region / identical protein binding / plasma membrane / cytoplasm Similarity search - Function
: / Aquaporin transporter / Major intrinsic protein, conserved site / MIP family signature. / Major intrinsic protein / Major intrinsic protein / Aquaporin-like Similarity search - Domain/homology
Journal: J Mol Biol / Year: 2010 Title: Influence of the cytoplasmic domains of aquaporin-4 on water conduction and array formation. Authors: Tadanori Mitsuma / Kazutoshi Tani / Yoko Hiroaki / Akiko Kamegawa / Hiroshi Suzuki / Hiroshi Hibino / Yoshihisa Kurachi / Yoshinori Fujiyoshi / Abstract: Phosphorylation of Ser180 in cytoplasmic loop D has been shown to reduce the water permeability of aquaporin (AQP) 4, the predominant water channel in the brain. However, when the structure of the ...Phosphorylation of Ser180 in cytoplasmic loop D has been shown to reduce the water permeability of aquaporin (AQP) 4, the predominant water channel in the brain. However, when the structure of the S180D mutant (AQP4M23S180D), which was generated to mimic phosphorylated Ser180, was determined to 2.8 Å resolution using electron diffraction patterns, it showed no significant differences from the structure of the wild-type channel. High-resolution density maps usually do not resolve protein regions that are only partially ordered, but these can sometimes be seen in lower-resolution density maps calculated from electron micrographs. We therefore used images of two-dimensional crystals and determined the structure of AQP4M23S180D at 10 A resolution. The features of the 10-A density map are consistent with those of the previously determined atomic model; in particular, there were no indications of any obstruction near the cytoplasmic pore entrance. In addition, water conductance measurements, both in vitro and in vivo, show the same water permeability for wild-type and mutant AQP4M23, suggesting that the S180D mutation neither reduces water conduction through a conformational change nor reduces water conduction by interacting with a protein that would obstruct the cytoplasmic channel entrance. Finally, the 10-A map shows a cytoplasmic density in between four adjacent tetramers that most likely represents the association of four N termini. This finding supports the critical role of the N terminus of AQP4 in the stabilization of orthogonal arrays, as well as their interference through lipid modification of cysteine residues in the longer N-terminal isoform.
History
Deposition
Jun 2, 2010
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Header (metadata) release
Jul 22, 2010
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Map release
Oct 4, 2010
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Update
Dec 26, 2012
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Current status
Dec 26, 2012
Processing site: RCSB / Status: Released
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Structure visualization
Movie
Surface view with section colored by density value
Details: molybdenum grid covered with a thin carbon film
Vitrification
Cryogen name: NITROGEN / Chamber temperature: 4.2 K / Instrument: REICHERT-JUNG PLUNGER / Details: Vitrification instrument: Reichert plunger Method: The grid was blotted with filter paper and plunged into liquid nitrogen.
Details
dialysis
Crystal formation
Details: dialysis
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Electron microscopy
Microscope
JEOL KYOTO-3000SFF
Temperature
Average: 4.2 K
Alignment procedure
Legacy - Astigmatism: bjective lens astigmatism was corrected at 400,000 times magnification
Image recording
Category: FILM / Film or detector model: TVIPS TEMCAM-F415 (4k x 4k) / Digitization - Scanner: OTHER / Digitization - Sampling interval: 15 µm / Number real images: 246 / Average electron dose: 38 e/Å2 / Bits/pixel: 16
Electron beam
Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Specimen holder: Top entry liquid helium cooled cryo specimen holder Specimen holder model: OTHER / Tilt angle min: -60 / Tilt angle max: 60 / Tilt series - Axis1 - Min angle: -60 ° / Tilt series - Axis1 - Max angle: 60 °
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Image processing
Final reconstruction
Algorithm: OTHER / Resolution.type: BY AUTHOR / Resolution: 10.0 Å / Resolution method: OTHER / Software - Name: MRC
Crystal parameters
Unit cell - A: 69.0 Å / Unit cell - B: 69.0 Å / Unit cell - C: 160.0 Å / Unit cell - γ: 90.0 ° / Unit cell - α: 90.0 ° / Unit cell - β: 90.0 ° / Plane group: P 4 21 2
CTF correction
Details: Each image
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