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- PDB-9bra: Intact V-ATPase State 2 and synaptophysin complex in mouse brain ... -

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Entry
Database: PDB / ID: 9bra
TitleIntact V-ATPase State 2 and synaptophysin complex in mouse brain isolated synaptic vesicles
Components
  • (V-type proton ATPase ...) x 14
  • Renin receptor cytoplasmic fragment
  • Ribonuclease kappa
  • Synaptophysin
KeywordsMEMBRANE PROTEIN / V-ATPase / synaptic vesicle
Function / homology
Function and homology information


Ion channel transport / regulation of opioid receptor signaling pathway / Amino acids regulate mTORC1 / clathrin-sculpted glutamate transport vesicle membrane / Transferrin endocytosis and recycling / Insulin receptor recycling / eye pigmentation / RHOA GTPase cycle / central nervous system maturation / Metabolism of Angiotensinogen to Angiotensins ...Ion channel transport / regulation of opioid receptor signaling pathway / Amino acids regulate mTORC1 / clathrin-sculpted glutamate transport vesicle membrane / Transferrin endocytosis and recycling / Insulin receptor recycling / eye pigmentation / RHOA GTPase cycle / central nervous system maturation / Metabolism of Angiotensinogen to Angiotensins / transporter activator activity / negative regulation of autophagic cell death / rostrocaudal neural tube patterning / cellular response to increased oxygen levels / positive regulation of transforming growth factor beta1 production / proton-transporting V-type ATPase, V1 domain / synaptic vesicle lumen acidification / endosome to plasma membrane protein transport / intracellular organelle / ROS and RNS production in phagocytes / proton-transporting V-type ATPase, V0 domain / extrinsic component of synaptic vesicle membrane / P-type proton-exporting transporter activity / plasma membrane proton-transporting V-type ATPase complex / lysosomal lumen acidification / clathrin-coated vesicle membrane / vacuolar proton-transporting V-type ATPase, V1 domain / endosomal lumen acidification / vacuolar proton-transporting V-type ATPase, V0 domain / vacuolar transport / proton-transporting V-type ATPase complex / neuron spine / head morphogenesis / protein localization to cilium / regulation of short-term neuronal synaptic plasticity / neuron projection terminus / vacuolar proton-transporting V-type ATPase complex / dendritic spine membrane / regulation of cellular pH / vacuolar acidification / syntaxin-1 binding / osteoclast development / regulation of synaptic vesicle exocytosis / : / cholesterol binding / ATPase complex / presynaptic active zone / regulation of neuronal synaptic plasticity / autophagosome membrane / microvillus / regulation of MAPK cascade / ATPase activator activity / synaptic vesicle endocytosis / excitatory synapse / cilium assembly / positive regulation of Wnt signaling pathway / transmembrane transporter complex / angiotensin maturation / regulation of macroautophagy / endomembrane system / axon terminus / ATP metabolic process / H+-transporting two-sector ATPase / proton transmembrane transport / ruffle / RNA endonuclease activity / phagocytic vesicle / Neutrophil degranulation / proton-transporting ATPase activity, rotational mechanism / endoplasmic reticulum-Golgi intermediate compartment membrane / SH2 domain binding / proton-transporting ATP synthase activity, rotational mechanism / SNARE binding / receptor-mediated endocytosis / secretory granule / regulation of long-term neuronal synaptic plasticity / Schaffer collateral - CA1 synapse / neuromuscular junction / terminal bouton / transmembrane transport / cilium / synaptic vesicle membrane / small GTPase binding / endocytosis / melanosome / positive regulation of canonical Wnt signaling pathway / synaptic vesicle / presynapse / apical part of cell / myelin sheath / presynaptic membrane / signaling receptor activity / cell body / ATPase binding / chemical synaptic transmission / postsynaptic membrane / intracellular iron ion homeostasis / receptor-mediated endocytosis of virus by host cell / Hydrolases; Acting on ester bonds / postsynaptic density
Similarity search - Function
Synaptophysin/synaptoporin / Synaptophysin / synaptoporin signature. / Marvel domain / Membrane-associating domain / MARVEL domain profile. / ATPase, V0 complex, subunit e1/e2, metazoa / V0 complex accessory subunit Ac45 / V-type proton ATPase subunit S1, luminal domain / V-type proton ATPase subunit S1, luminal domain / Renin receptor-like ...Synaptophysin/synaptoporin / Synaptophysin / synaptoporin signature. / Marvel domain / Membrane-associating domain / MARVEL domain profile. / ATPase, V0 complex, subunit e1/e2, metazoa / V0 complex accessory subunit Ac45 / V-type proton ATPase subunit S1, luminal domain / V-type proton ATPase subunit S1, luminal domain / Renin receptor-like / Renin receptor-like protein / ATPase, V1 complex, subunit H / ATPase, V1 complex, subunit H, C-terminal / ATPase, V1 complex, subunit H, C-terminal domain superfamily / V-ATPase subunit H / V-ATPase subunit H / ATPase, V1 complex, subunit A / Ribonuclease kappa / V-type proton ATPase subunit S1/VOA1, transmembrane domain / V0 complex accessory subunit Ac45/VOA1 transmembrane domain / ATPase, V1 complex, subunit C / Vacuolar ATP synthase subunit C superfamily / V-ATPase subunit C / Vacuolar (H+)-ATPase G subunit / Vacuolar (H+)-ATPase G subunit / ATPase, V1 complex, subunit B / ATPase, V1 complex, subunit F, eukaryotic / ATPase, V0 complex, subunit e1/e2 / ATP synthase subunit H / ATPase, V0 complex, subunit d / V-ATPase proteolipid subunit C, eukaryotic / ATPase, V0 complex, subunit 116kDa, eukaryotic / V-ATPase proteolipid subunit / ATPase, V0 complex, c/d subunit / V-type ATPase subunit C/d / V-type ATP synthase subunit c/d subunit superfamily / V-type ATP synthase c/d subunit, domain 3 superfamily / ATP synthase (C/AC39) subunit / V-type ATPase, V0 complex, 116kDa subunit family / V-type ATPase 116kDa subunit family / V-type ATPase subunit E / V-type ATPase subunit E, C-terminal domain superfamily / ATP synthase (E/31 kDa) subunit / ATPase, V1 complex, subunit D / ATPase, V1 complex, subunit F / ATPase, V1 complex, subunit F superfamily / ATP synthase subunit D / ATP synthase (F/14-kDa) subunit / V-type ATP synthase regulatory subunit B/beta / V-type ATP synthase catalytic alpha chain / ATPsynthase alpha/beta subunit, N-terminal extension / ATPsynthase alpha/beta subunit N-term extension / V-ATPase proteolipid subunit C-like domain / F/V-ATP synthase subunit C superfamily / ATP synthase subunit C / ATPase, F1/V1 complex, beta/alpha subunit, C-terminal / ATP synthase subunit alpha, N-terminal domain-like superfamily / ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain superfamily / ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain / ATP synthase alpha/beta family, beta-barrel domain / ATPase, alpha/beta subunit, nucleotide-binding domain, active site / ATP synthase alpha and beta subunits signature. / ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain / ATP synthase alpha/beta family, nucleotide-binding domain / Armadillo-like helical / Armadillo-type fold / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
V-type proton ATPase catalytic subunit A / V-type proton ATPase subunit E 1 / V-type proton ATPase subunit d 1 / V-type proton ATPase subunit D / V-type proton ATPase subunit B, brain isoform / V-type proton ATPase 16 kDa proteolipid subunit c / Synaptophysin / V-type proton ATPase subunit H / Ribonuclease kappa / V-type proton ATPase 21 kDa proteolipid subunit c'' ...V-type proton ATPase catalytic subunit A / V-type proton ATPase subunit E 1 / V-type proton ATPase subunit d 1 / V-type proton ATPase subunit D / V-type proton ATPase subunit B, brain isoform / V-type proton ATPase 16 kDa proteolipid subunit c / Synaptophysin / V-type proton ATPase subunit H / Ribonuclease kappa / V-type proton ATPase 21 kDa proteolipid subunit c'' / V-type proton ATPase subunit e 2 / Renin receptor / V-type proton ATPase subunit F / V-type proton ATPase subunit S1 / V-type proton ATPase subunit G 2 / V-type proton ATPase subunit C 1 / V-type proton ATPase 116 kDa subunit a 1
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.3 Å
AuthorsWang, C. / Jiang, W. / Yang, K. / Wang, X. / Guo, Q. / Brunger, A.T.
Funding support United States, 2items
OrganizationGrant numberCountry
Howard Hughes Medical Institute (HHMI) United States
National Institutes of Health/National Institute of Mental Health (NIH/NIMH)RO1MH63105 United States
CitationJournal: Nature / Year: 2024
Title: Structure and topography of the synaptic V-ATPase-synaptophysin complex.
Authors: Chuchu Wang / Wenhong Jiang / Jeremy Leitz / Kailu Yang / Luis Esquivies / Xing Wang / Xiaotao Shen / Richard Held / Daniel J Adams / Tamara Basta / Lucas Hampton / Ruiqi Jian / Lihua Jiang ...Authors: Chuchu Wang / Wenhong Jiang / Jeremy Leitz / Kailu Yang / Luis Esquivies / Xing Wang / Xiaotao Shen / Richard Held / Daniel J Adams / Tamara Basta / Lucas Hampton / Ruiqi Jian / Lihua Jiang / Michael H B Stowell / Wolfgang Baumeister / Qiang Guo / Axel T Brunger /
Abstract: Synaptic vesicles are organelles with a precisely defined protein and lipid composition, yet the molecular mechanisms for the biogenesis of synaptic vesicles are mainly unknown. Here, we discovered a ...Synaptic vesicles are organelles with a precisely defined protein and lipid composition, yet the molecular mechanisms for the biogenesis of synaptic vesicles are mainly unknown. Here, we discovered a well-defined interface between the synaptic vesicle V-ATPase and synaptophysin by in situ cryo-electron tomography and single particle cryo-electron microscopy of functional synaptic vesicles isolated from mouse brains. The synaptic vesicle V-ATPase is an ATP-dependent proton pump that establishes the protein gradient across the synaptic vesicle, which in turn drives the uptake of neurotransmitters. Synaptophysin and its paralogs synaptoporin and synaptogyrin belong to a family of abundant synaptic vesicle proteins whose function is still unclear. We performed structural and functional studies of synaptophysin knockout mice, confirming the identity of synaptophysin as an interaction partner with the V-ATPase. Although there is little change in the conformation of the V-ATPase upon interaction with synaptophysin, the presence of synaptophysin in synaptic vesicles profoundly affects the copy number of V-ATPases. This effect on the topography of synaptic vesicles suggests that synaptophysin assists in their biogenesis. In support of this model, we observed that synaptophysin knockout mice exhibit severe seizure susceptibility, suggesting an imbalance of neurotransmitter release as a physiological consequence of the absence of synaptophysin.
History
DepositionMay 11, 2024Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 19, 2024Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
8: V-type proton ATPase subunit E 1
R: V-type proton ATPase subunit G 2
9: V-type proton ATPase subunit E 1
T: V-type proton ATPase subunit G 2
Q: V-type proton ATPase subunit E 1
V: V-type proton ATPase subunit G 2
0: V-type proton ATPase catalytic subunit A
1: V-type proton ATPase catalytic subunit A
2: V-type proton ATPase catalytic subunit A
3: V-type proton ATPase subunit B, brain isoform
4: V-type proton ATPase subunit B, brain isoform
5: V-type proton ATPase subunit B, brain isoform
6: V-type proton ATPase subunit C 1
7: V-type proton ATPase subunit D
U: V-type proton ATPase subunit H
X: V-type proton ATPase subunit F
a: V-type proton ATPase 116 kDa subunit a 1
b: V-type proton ATPase 21 kDa proteolipid subunit c''
d: V-type proton ATPase subunit d 1
g: V-type proton ATPase 16 kDa proteolipid subunit c
h: V-type proton ATPase 16 kDa proteolipid subunit c
i: V-type proton ATPase 16 kDa proteolipid subunit c
j: V-type proton ATPase 16 kDa proteolipid subunit c
k: V-type proton ATPase 16 kDa proteolipid subunit c
l: V-type proton ATPase 16 kDa proteolipid subunit c
m: V-type proton ATPase 16 kDa proteolipid subunit c
n: V-type proton ATPase 16 kDa proteolipid subunit c
o: V-type proton ATPase 16 kDa proteolipid subunit c
p: Renin receptor cytoplasmic fragment
c: V-type proton ATPase subunit S1
f: Ribonuclease kappa
s: Synaptophysin
e: V-type proton ATPase subunit e 2


Theoretical massNumber of molelcules
Total (without water)1,081,50233
Polymers1,081,50233
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

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V-type proton ATPase ... , 14 types, 30 molecules 89QRTV01234567UXabdghijklmnoce

#1: Protein V-type proton ATPase subunit E 1 / V-ATPase subunit E 1 / V-ATPase 31 kDa subunit / p31 / Vacuolar proton pump subunit E 1


Mass: 26196.449 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Details: VATE1_MOUSE V-type proton ATPase subunit E 1 / Source: (natural) Mus musculus (house mouse) / References: UniProt: P50518
#2: Protein V-type proton ATPase subunit G 2 / V-ATPase subunit G 2 / V-ATPase 13 kDa subunit 2 / Vacuolar proton pump subunit G 2


Mass: 13674.476 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Details: VATG2_MOUSE V-type proton ATPase subunit G 2 / Source: (natural) Mus musculus (house mouse) / References: UniProt: Q9WTT4
#3: Protein V-type proton ATPase catalytic subunit A / V-ATPase subunit A / V-ATPase 69 kDa subunit / Vacuolar proton pump subunit alpha


Mass: 68402.875 Da / Num. of mol.: 3 / Source method: isolated from a natural source
Details: VATA_MOUSE V-type proton ATPase catalytic subunit A
Source: (natural) Mus musculus (house mouse)
References: UniProt: P50516, H+-transporting two-sector ATPase
#4: Protein V-type proton ATPase subunit B, brain isoform / V-ATPase subunit B 2 / Endomembrane proton pump 58 kDa subunit / Vacuolar proton pump subunit B 2


Mass: 56611.570 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Details: VATB2_MOUSE V-type proton ATPase subunit B / Source: (natural) Mus musculus (house mouse) / References: UniProt: P62814
#5: Protein V-type proton ATPase subunit C 1 / V-ATPase subunit C 1 / Vacuolar proton pump subunit C 1


Mass: 43945.449 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: VATC1_MOUSE V-type proton ATPase subunit C 1 / Source: (natural) Mus musculus (house mouse) / References: UniProt: Q9Z1G3
#6: Protein V-type proton ATPase subunit D / V-ATPase subunit D / V-ATPase 28 kDa accessory protein / Vacuolar proton pump subunit D


Mass: 28419.117 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: VATD_MOUSE V-type proton ATPase subunit D / Source: (natural) Mus musculus (house mouse) / References: UniProt: P57746
#7: Protein V-type proton ATPase subunit H / V-ATPase subunit H / Vacuolar proton pump subunit H


Mass: 55922.859 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: VATH_MOUSE V-type proton ATPase subunit H / Source: (natural) Mus musculus (house mouse) / References: UniProt: Q8BVE3
#8: Protein V-type proton ATPase subunit F / V-ATPase subunit F / V-ATPase 14 kDa subunit / Vacuolar proton pump subunit F


Mass: 13389.262 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: VATF_MOUSE V-type proton ATPase subunit F / Source: (natural) Mus musculus (house mouse) / References: UniProt: Q9D1K2
#9: Protein V-type proton ATPase 116 kDa subunit a 1 / V-ATPase 116 kDa subunit a 1 / Clathrin-coated vesicle/synaptic vesicle proton pump 116 kDa subunit ...V-ATPase 116 kDa subunit a 1 / Clathrin-coated vesicle/synaptic vesicle proton pump 116 kDa subunit / Vacuolar adenosine triphosphatase subunit Ac116 / Vacuolar proton pump subunit 1 / Vacuolar proton translocating ATPase 116 kDa subunit a isoform 1


Mass: 96442.500 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Details: VPP1_MOUSE V-type proton ATPase 116 kDa subunit a isoform 1
Source: (natural) Mus musculus (house mouse) / References: UniProt: Q9Z1G4
#10: Protein V-type proton ATPase 21 kDa proteolipid subunit c'' / V-ATPase 21 kDa proteolipid subunit c'' / 23 kDa subunit of V-ATPase / Vacuolar proton pump 21 kDa ...V-ATPase 21 kDa proteolipid subunit c'' / 23 kDa subunit of V-ATPase / Vacuolar proton pump 21 kDa proteolipid subunit c''


Mass: 21618.553 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Details: VATO_MOUSE V-type proton ATPase 21 kDa proteolipid subunit
Source: (natural) Mus musculus (house mouse) / References: UniProt: Q91V37
#11: Protein V-type proton ATPase subunit d 1 / V-ATPase subunit d 1 / P39 / Physophilin / V-ATPase 40 kDa accessory protein / V-ATPase AC39 ...V-ATPase subunit d 1 / P39 / Physophilin / V-ATPase 40 kDa accessory protein / V-ATPase AC39 subunit / Vacuolar proton pump subunit d 1


Mass: 40341.934 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: VA0D1_MOUSE V-type proton ATPase subunit d 1 / Source: (natural) Mus musculus (house mouse) / References: UniProt: P51863
#12: Protein
V-type proton ATPase 16 kDa proteolipid subunit c / V-ATPase 16 kDa proteolipid subunit c / PL16 / Vacuolar proton pump 16 kDa proteolipid subunit c


Mass: 15815.833 Da / Num. of mol.: 9 / Source method: isolated from a natural source
Details: VATL_MOUSE V-type proton ATPase 16 kDa proteolipid subunit
Source: (natural) Mus musculus (house mouse) / References: UniProt: P63082
#14: Protein V-type proton ATPase subunit S1 / V-ATPase subunit S1 / Protein C7-1 / V-ATPase Ac45 subunit / V-ATPase S1 accessory protein / ...V-ATPase subunit S1 / Protein C7-1 / V-ATPase Ac45 subunit / V-ATPase S1 accessory protein / Vacuolar proton pump subunit S1


Mass: 51046.215 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: VAS1_MOUSE V-type proton ATPase subunit S1 / Source: (natural) Mus musculus (house mouse) / References: UniProt: Q9R1Q9
#17: Protein V-type proton ATPase subunit e 2 / V-ATPase subunit e 2 / Vacuolar proton pump subunit e 2


Mass: 9203.020 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: VA0E2_MOUSE V-type proton ATPase subunit e 2 / Source: (natural) Mus musculus (house mouse) / References: UniProt: Q91XE7

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Protein , 3 types, 3 molecules pfs

#13: Protein Renin receptor cytoplasmic fragment


Mass: 39128.789 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: RENR_MOUSE Renin receptor / Source: (natural) Mus musculus (house mouse) / References: UniProt: Q9CYN9
#15: Protein Ribonuclease kappa / RNase K / RNase kappa / V-type proton ATPase subunit f / V-ATPase subunit f


Mass: 11000.004 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: RNK_MOUSE Ribonuclease kappa / Source: (natural) Mus musculus (house mouse)
References: UniProt: Q8K3C0, Hydrolases; Acting on ester bonds
#16: Protein Synaptophysin / BM89 antigen / Major synaptic vesicle protein p38


Mass: 34045.406 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: SYPH_MOUSE Synaptophysin / Source: (natural) Mus musculus (house mouse) / References: UniProt: Q62277

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Experimental details

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Experiment

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

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Sample preparation

ComponentName: Mouse brain isolated glutamatergic synaptic vesicles / Type: ORGANELLE OR CELLULAR COMPONENT / Entity ID: all / Source: NATURAL
Molecular weightExperimental value: NO
Source (natural)Organism: Mus musculus (house mouse)
Buffer solutionpH: 7.4
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Details: The specimen state should be an intact subcellular component.
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 4000 nm / Nominal defocus min: 1000 nm
Image recordingElectron dose: 50 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k)

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Processing

SoftwareName: PHENIX / Version: 1.21_5207: / Classification: refinement
EM software
IDNameCategory
7Cootmodel fitting
9PHENIXmodel refinement
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 4.3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 25667 / Symmetry type: POINT
Atomic model buildingProtocol: FLEXIBLE FIT

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