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- PDB-8gs3: Cryo-EM structure of human Neuroligin 3 -

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Basic information

Entry
Database: PDB / ID: 8gs3
TitleCryo-EM structure of human Neuroligin 3
ComponentsNeuroligin-3NLGN3
KeywordsMEMBRANE PROTEIN / Neuroligin / synapse protein / plasma membrane
Function / homology
Function and homology information


asymmetric, glutamatergic, excitatory synapse / symmetric, GABA-ergic, inhibitory synapse / rhythmic synaptic transmission / postsynaptic membrane assembly / presynaptic membrane assembly / regulation of respiratory gaseous exchange by nervous system process / neuron cell-cell adhesion / presynapse assembly / neurexin family protein binding / vocalization behavior ...asymmetric, glutamatergic, excitatory synapse / symmetric, GABA-ergic, inhibitory synapse / rhythmic synaptic transmission / postsynaptic membrane assembly / presynaptic membrane assembly / regulation of respiratory gaseous exchange by nervous system process / neuron cell-cell adhesion / presynapse assembly / neurexin family protein binding / vocalization behavior / inhibitory postsynaptic potential / axon extension / Neurexins and neuroligins / positive regulation of synapse assembly / positive regulation of AMPA receptor activity / adult behavior / social behavior / positive regulation of excitatory postsynaptic potential / synaptic vesicle endocytosis / excitatory synapse / endocytic vesicle / cell adhesion molecule binding / synapse assembly / receptor-mediated endocytosis / positive regulation of synaptic transmission, glutamatergic / learning / synapse organization / modulation of chemical synaptic transmission / presynapse / signaling receptor activity / scaffold protein binding / chemical synaptic transmission / postsynaptic membrane / molecular adaptor activity / synapse / cell surface / membrane / plasma membrane
Similarity search - Function
Neuroligin / Carboxylesterase type B, conserved site / Carboxylesterases type-B signature 2. / Carboxylesterase, type B / Carboxylesterase family / Alpha/Beta hydrolase fold
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.9 Å
AuthorsZhang, H. / Zhang, Z. / Hou, M.
Funding support China, 1items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC) China
CitationJournal: Front Endocrinol (Lausanne) / Year: 2022
Title: Expression and structural analysis of human neuroligin 2 and neuroligin 3 implicated in autism spectrum disorders.
Authors: Zhenzhen Zhang / Mengzhuo Hou / Huaxing Ou / Daping Wang / Zhifang Li / Huawei Zhang / Jianping Lu /
Abstract: The development of autism spectrum disorders (ASDs) involves both environmental factors such as maternal diabetes and genetic factors such as neuroligins (NLGNs). NLGN2 and NLGN3 are two members of ...The development of autism spectrum disorders (ASDs) involves both environmental factors such as maternal diabetes and genetic factors such as neuroligins (NLGNs). NLGN2 and NLGN3 are two members of NLGNs with distinct distributions and functions in synapse development and plasticity. The relationship between maternal diabetes and NLGNs, and the distinct working mechanisms of different NLGNs currently remain unclear. Here, we first analyzed the expression levels of NLGN2 and NLGN3 in a streptozotocin-induced ASD mouse model and different brain regions to reveal their differences and similarities. Then, cryogenic electron microscopy (cryo-EM) structures of human NLGN2 and NLGN3 were determined. The overall structures are similar to their homologs in previous reports. However, structural comparisons revealed the relative rotations of two protomers in the homodimers of NLGN2 and NLGN3. Taken together with the previously reported NLGN2-MDGA1 complex, we speculate that the distinct assembly adopted by NLGN2 and NLGN3 may affect their interactions with MDGAs. Our results provide structural insights into the potential distinct mechanisms of NLGN2 and NLGN3 implicated in the development of ASD.
History
DepositionSep 4, 2022Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Sep 20, 2023Provider: repository / Type: Initial release
Revision 1.1Apr 3, 2024Group: Data collection / Database references / Structure summary
Category: audit_author / citation ...audit_author / citation / citation_author / em_author_list
Item: _audit_author.name / _citation.country ..._audit_author.name / _citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _em_author_list.author

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Neuroligin-3
B: Neuroligin-3


Theoretical massNumber of molelcules
Total (without water)187,9982
Polymers187,9982
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: electron microscopy
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

#1: Protein Neuroligin-3 / NLGN3 / Gliotactin homolog


Mass: 93999.062 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: NLGN3, NL3 / Cell line (production host): HEK293 / Production host: Homo sapiens (human) / References: UniProt: Q9NZ94

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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: homodimer of Neuroligin 3 / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT
Source (natural)Organism: Homo sapiens (human)
Source (recombinant)Organism: Homo sapiens (human) / Cell: HEK293
Buffer solutionpH: 7.4
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 FIELDBright-field microscopy / Nominal defocus max: 2500 nm / Nominal defocus min: 1500 nm / Calibrated defocus min: 1500 nm
Image recordingElectron dose: 50 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k)

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Processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 3.9 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 255939 / Symmetry type: POINT
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.0138626
ELECTRON MICROSCOPYf_angle_d1.2911790
ELECTRON MICROSCOPYf_dihedral_angle_d4.7831157
ELECTRON MICROSCOPYf_chiral_restr0.0471277
ELECTRON MICROSCOPYf_plane_restr0.0071539

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