+Open data
-Basic information
Entry | Database: PDB / ID: 8ben | ||||||
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Title | LRR domain Structure of the LRRC8C protein | ||||||
Components | Volume-regulated anion channel subunit LRRC8C | ||||||
Keywords | MEMBRANE PROTEIN / Ion channel / Volume-regulated anion channel | ||||||
Function / homology | Function and homology information Miscellaneous transport and binding events / volume-sensitive anion channel activity / taurine transmembrane transport / monoatomic anion transmembrane transport / aspartate transmembrane transport / cyclic-GMP-AMP transmembrane import across plasma membrane / cellular response to osmotic stress / protein hexamerization / monoatomic ion channel complex / fat cell differentiation ...Miscellaneous transport and binding events / volume-sensitive anion channel activity / taurine transmembrane transport / monoatomic anion transmembrane transport / aspartate transmembrane transport / cyclic-GMP-AMP transmembrane import across plasma membrane / cellular response to osmotic stress / protein hexamerization / monoatomic ion channel complex / fat cell differentiation / endoplasmic reticulum membrane / endoplasmic reticulum / signal transduction / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.1 Å | ||||||
Authors | Sawicka, M. / Dutzler, R. | ||||||
Funding support | Switzerland, 1items
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Citation | Journal: Nat Struct Mol Biol / Year: 2023 Title: Structure of a volume-regulated heteromeric LRRC8A/C channel. Authors: Sonja Rutz / Dawid Deneka / Antje Dittmann / Marta Sawicka / Raimund Dutzler / Abstract: Volume-regulated anion channels (VRACs) participate in the cellular response to osmotic swelling. These membrane proteins consist of heteromeric assemblies of LRRC8 subunits, whose compositions ...Volume-regulated anion channels (VRACs) participate in the cellular response to osmotic swelling. These membrane proteins consist of heteromeric assemblies of LRRC8 subunits, whose compositions determine permeation properties. Although structures of the obligatory LRRC8A, also referred to as SWELL1, have previously defined the architecture of VRACs, the organization of heteromeric channels has remained elusive. Here we have addressed this question by the structural characterization of murine LRRC8A/C channels. Like LRRC8A, these proteins assemble as hexamers. Despite 12 possible arrangements, we find a predominant organization with an A:C ratio of two. In this assembly, four LRRC8A subunits cluster in their preferred conformation observed in homomers, as pairs of closely interacting proteins that stabilize a closed state of the channel. In contrast, the two interacting LRRC8C subunits show a larger flexibility, underlining their role in the destabilization of the tightly packed A subunits, thereby enhancing the activation properties of the protein. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 8ben.cif.gz | 324.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb8ben.ent.gz | 260.2 KB | Display | PDB format |
PDBx/mmJSON format | 8ben.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/be/8ben ftp://data.pdbj.org/pub/pdb/validation_reports/be/8ben | HTTPS FTP |
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-Related structure data
Related structure data | 8b40C 8b41C 8b42C 6fnwS C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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2 |
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3 |
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4 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments:
NCS oper:
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-Components
#1: Protein | Mass: 47189.094 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Lrrc8c, Ad158, Fad158 / Production host: Homo sapiens (human) / References: UniProt: Q8R502 |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.27 Å3/Da / Density % sol: 45.78 % |
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Crystal grow | Temperature: 277.15 K / Method: vapor diffusion, sitting drop / Details: 0.2 M magnesium chloride, 20% PEG3350 |
-Data collection
Diffraction | Mean temperature: 80 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 1 Å |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Feb 23, 2017 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 3.1→49.19 Å / Num. obs: 30438 / % possible obs: 98.3 % / Redundancy: 7.2 % / Biso Wilson estimate: 30.53 Å2 / Rmerge(I) obs: 0.35 / Net I/σ(I): 5.53 |
Reflection shell | Resolution: 3.1→3.2 Å / Num. unique obs: 2773 / CC1/2: 0.76 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 6FNW Resolution: 3.1→49.19 Å / SU ML: 0.4184 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 29.7431 Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 26.32 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.1→49.19 Å
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Refine LS restraints |
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Refine LS restraints NCS |
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LS refinement shell |
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