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- PDB-6jpf: Structure of atOSCA1.1 channel at 3.52A -

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Basic information

Entry
Database: PDB / ID: 6jpf
TitleStructure of atOSCA1.1 channel at 3.52A
ComponentsProtein OSCA1
KeywordsMETAL TRANSPORT / osca / TMEM63 / ion channel / mechanosensitive / membrane protein / osmosensing
Function / homology
Function and homology information


regulation of calcium ion import / mechanosensitive monoatomic ion channel activity / calcium-activated cation channel activity / cellular hyperosmotic response / response to osmotic stress / monoatomic cation channel activity / protein tetramerization / plasma membrane / cytosol
Similarity search - Function
CSC1/OSCA1-like, 7TM region / CSC1/OSCA1-like, cytosolic domain / CSC1/OSCA1-like, N-terminal transmembrane domain / Calcium permeable stress-gated cation channel 1-like / Calcium-dependent channel, 7TM region, putative phosphate / Late exocytosis, associated with Golgi transport / Cytosolic domain of 10TM putative phosphate transporter
Similarity search - Domain/homology
Hyperosmolality-gated Ca2+ permeable channel 1.1
Similarity search - Component
Biological speciesArabidopsis thaliana (thale cress)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.52 Å
AuthorsChen, L. / Zhang, M. / Kang, Y. / Wu, J.X.
Funding support China, 3items
OrganizationGrant numberCountry
National Natural Science Foundation of China31622021 China
National Natural Science Foundation of China31521062 China
Ministry of Science and Technology (China)2016YFA0502004 China
CitationJournal: Nat Struct Mol Biol / Year: 2018
Title: Structure of the mechanosensitive OSCA channels.
Authors: Mingfeng Zhang / Dali Wang / Yunlu Kang / Jing-Xiang Wu / Fuqiang Yao / Chengfang Pan / Zhiqiang Yan / Chen Song / Lei Chen /
Abstract: Mechanosensitive ion channels convert mechanical stimuli into a flow of ions. These channels are widely distributed from bacteria to higher plants and humans, and are involved in many crucial ...Mechanosensitive ion channels convert mechanical stimuli into a flow of ions. These channels are widely distributed from bacteria to higher plants and humans, and are involved in many crucial physiological processes. Here we show that two members of the OSCA protein family in Arabidopsis thaliana, namely AtOSCA1.1 and AtOSCA3.1, belong to a new class of mechanosensitive ion channels. We solve the structure of the AtOSCA1.1 channel at 3.5-Å resolution and AtOSCA3.1 at 4.8-Å resolution by cryo-electron microscopy. OSCA channels are symmetric dimers that are mediated by cytosolic inter-subunit interactions. Strikingly, they have structural similarity to the mammalian TMEM16 family proteins. Our structural analysis accompanied with electrophysiological studies identifies the ion permeation pathway within each subunit and suggests a conformational change model for activation.
History
DepositionMar 26, 2019Deposition site: PDBJ / Processing site: PDBJ
SupersessionApr 10, 2019ID: 5YD1
Revision 1.0Apr 10, 2019Provider: repository / Type: Initial release
Revision 1.1Dec 25, 2019Group: Database references / Category: pdbx_database_related
Revision 1.2Mar 27, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Assembly

Deposited unit
A: Protein OSCA1
B: Protein OSCA1


Theoretical massNumber of molelcules
Total (without water)175,3942
Polymers175,3942
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_5551
Buried area2660 Å2
ΔGint-11 kcal/mol
Surface area51260 Å2

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Components

#1: Protein Protein OSCA1 / CSC1-like protein At4g04340 / Protein reduced hyperosmolality-induced [Ca(2+)]i increase 1


Mass: 87697.008 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Gene: OSCA1, At4g04340, T19B17.6 / Production host: Homo sapiens (human) / References: UniProt: Q9XEA1

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: atOSCA1.1 channel in detergent / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT
Source (natural)Organism: Arabidopsis thaliana (thale cress)
Source (recombinant)Organism: Homo sapiens (human)
Buffer solutionpH: 8
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD
Image recordingElectron dose: 50 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k)

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Processing

CTF correctionType: NONE
3D reconstructionResolution: 3.52 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 115697 / Symmetry type: POINT

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