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- PDB-8qju: Structure of the human 1-phosphatidylinositol 4,5-bisphosphate ph... -

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Basic information

Entry
Database: PDB / ID: 8qju
TitleStructure of the human 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2 (PLCG2) protein
Components1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2
KeywordsLIPID BINDING PROTEIN / Lipid metabolism
Function / homology
Function and homology information


follicular B cell differentiation / inositol trisphosphate biosynthetic process / regulation of calcineurin-NFAT signaling cascade / positive regulation of dendritic cell cytokine production / phosphoinositide phospholipase C / antifungal innate immune response / positive regulation of interleukin-23 production / cellular response to lectin / response to yeast / phosphorylation-dependent protein binding ...follicular B cell differentiation / inositol trisphosphate biosynthetic process / regulation of calcineurin-NFAT signaling cascade / positive regulation of dendritic cell cytokine production / phosphoinositide phospholipase C / antifungal innate immune response / positive regulation of interleukin-23 production / cellular response to lectin / response to yeast / phosphorylation-dependent protein binding / positive regulation of cell cycle G1/S phase transition / Toll Like Receptor 4 (TLR4) Cascade / phosphatidylinositol metabolic process / positive regulation of phagocytosis, engulfment / positive regulation of neuroinflammatory response / cell activation / Erythropoietin activates Phospholipase C gamma (PLCG) / phospholipase C activity / phosphatidylinositol-4,5-bisphosphate phospholipase C activity / phosphatidylinositol biosynthetic process / programmed cell death / macrophage activation involved in immune response / phospholipid catabolic process / cellular response to lipid / regulation of canonical NF-kappaB signal transduction / negative regulation of programmed cell death / positive regulation of macrophage cytokine production / toll-like receptor signaling pathway / phosphatidylinositol-mediated signaling / positive regulation of reactive oxygen species biosynthetic process / intracellular vesicle / Dectin-2 family / positive regulation of NLRP3 inflammasome complex assembly / Synthesis of IP3 and IP4 in the cytosol / stimulatory C-type lectin receptor signaling pathway / Fc-epsilon receptor signaling pathway / B cell activation / regulation of lipid metabolic process / positive regulation of interleukin-10 production / positive regulation of receptor internalization / Generation of second messenger molecules / positive regulation of epithelial cell migration / positive regulation of type I interferon production / response to axon injury / Role of phospholipids in phagocytosis / GPVI-mediated activation cascade / release of sequestered calcium ion into cytosol / phosphotyrosine residue binding / positive regulation of interleukin-12 production / FCERI mediated Ca+2 mobilization / positive regulation of interleukin-2 production / B cell differentiation / FCGR3A-mediated IL10 synthesis / positive regulation of calcium-mediated signaling / cellular response to calcium ion / lipopolysaccharide-mediated signaling pathway / Antigen activates B Cell Receptor (BCR) leading to generation of second messengers / positive regulation of DNA-binding transcription factor activity / protein tyrosine kinase binding / B cell receptor signaling pathway / FCERI mediated MAPK activation / calcium-mediated signaling / platelet activation / positive regulation of interleukin-6 production / CLEC7A (Dectin-1) signaling / Wnt signaling pathway / ruffle membrane / Signaling by CSF1 (M-CSF) in myeloid cells / positive regulation of tumor necrosis factor production / DAP12 signaling / T cell receptor signaling pathway / scaffold protein binding / Potential therapeutics for SARS / positive regulation of MAPK cascade / intracellular signal transduction / membrane raft / positive regulation of gene expression / protein kinase binding / perinuclear region of cytoplasm / extracellular exosome / plasma membrane / cytosol / cytoplasm
Similarity search - Function
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2, SH3 domain / Phosphatidylinositol-4, 5-bisphosphate phosphodiesterase gamma / PLC-gamma, C-terminal SH2 domain / PLC-gamma, N-terminal SH2 domain / PLCG EF-hand motif 2 / Pleckstrin homology domain / Phosphoinositide phospholipase C family / Phospholipase C, phosphatidylinositol-specific, Y domain / Phosphatidylinositol-specific phospholipase C, Y domain / Phosphatidylinositol-specific phospholipase Y-box domain profile. ...1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2, SH3 domain / Phosphatidylinositol-4, 5-bisphosphate phosphodiesterase gamma / PLC-gamma, C-terminal SH2 domain / PLC-gamma, N-terminal SH2 domain / PLCG EF-hand motif 2 / Pleckstrin homology domain / Phosphoinositide phospholipase C family / Phospholipase C, phosphatidylinositol-specific, Y domain / Phosphatidylinositol-specific phospholipase C, Y domain / Phosphatidylinositol-specific phospholipase Y-box domain profile. / Phospholipase C, catalytic domain (part); domain Y / Phosphatidylinositol-specific phospholipase C, X domain / Phosphatidylinositol-specific phospholipase C, X domain / Phospholipase C, catalytic domain (part); domain X / Phosphatidylinositol-specific phospholipase X-box domain profile. / PLC-like phosphodiesterase, TIM beta/alpha-barrel domain superfamily / Protein kinase C conserved region 2 (CalB) / C2 domain / C2 domain / C2 domain profile. / C2 domain superfamily / PH domain profile. / Pleckstrin homology domain. / Pleckstrin homology domain / SH3 domain / SH2 domain / Src homology 2 (SH2) domain profile. / Src homology 2 domains / SH2 domain / SH2 domain superfamily / Src homology 3 domains / SH3-like domain superfamily / Src homology 3 (SH3) domain profile. / SH3 domain / EF-hand domain pair / PH-like domain superfamily
Similarity search - Domain/homology
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.5 Å
AuthorsFaille, A. / Warren, A.J.
Funding support United Kingdom, 1items
OrganizationGrant numberCountry
Medical Research Council (MRC, United Kingdom) United Kingdom
CitationJournal: To Be Published
Title: Structure of human PLCG2
Authors: Faille, A.J. / Qamar, S. / Warren, A.J. / St George-Hyslop, P.
History
DepositionSep 13, 2023Deposition site: PDBE / Processing site: PDBE
Revision 1.0Mar 26, 2025Provider: repository / Type: Initial release
Revision 1.0Mar 26, 2025Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release
Revision 1.0Mar 26, 2025Data content type: FSC / Data content type: FSC / Provider: repository / Type: Initial release
Revision 1.0Mar 26, 2025Data content type: Half map / Part number: 1 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Mar 26, 2025Data content type: Half map / Part number: 2 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Mar 26, 2025Data content type: Image / Data content type: Image / Provider: repository / Type: Initial release
Revision 1.0Mar 26, 2025Data content type: Mask / Part number: 1 / Data content type: Mask / Provider: repository / Type: Initial release
Revision 1.0Mar 26, 2025Data content type: Primary map / Data content type: Primary map / Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2


Theoretical massNumber of molelcules
Total (without water)148,0751
Polymers148,0751
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1

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Components

#1: Protein 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2


Mass: 148074.578 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PLCG2 / Production host: Homo sapiens (human) / References: UniProt: P16885
Has protein modificationY

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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: 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2
Type: CELL / Entity ID: all / Source: NATURAL
Source (natural)Organism: Homo sapiens (human)
Buffer solutionpH: 7.5
SpecimenConc.: 1.5 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportGrid material: GOLD / Grid mesh size: 300 divisions/in. / Grid type: UltrAuFoil R0./1
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: 2400 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

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 130911 / Symmetry type: POINT
RefinementResolution: 3.5→3.5 Å / Cor.coef. Fo:Fc: 0.859 / SU B: 17.532 / SU ML: 0.297 / ESU R: 0.435
Stereochemistry target values: MAXIMUM LIKELIHOOD WITH PHASES
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflection
Rwork0.39488 --
obs0.39488 107886 100 %
Solvent computationSolvent model: PARAMETERS FOR MASK CACLULATION
Displacement parametersBiso mean: 244.72 Å2
Refinement stepCycle: 1 / Total: 9441
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
ELECTRON MICROSCOPYr_bond_refined_d0.0080.0129665
ELECTRON MICROSCOPYr_bond_other_d00.0169057
ELECTRON MICROSCOPYr_angle_refined_deg1.2161.65413055
ELECTRON MICROSCOPYr_angle_other_deg0.4211.57520916
ELECTRON MICROSCOPYr_dihedral_angle_1_deg4.97251148
ELECTRON MICROSCOPYr_dihedral_angle_2_deg3.407572
ELECTRON MICROSCOPYr_dihedral_angle_3_deg25.303101751
ELECTRON MICROSCOPYr_dihedral_angle_4_deg
ELECTRON MICROSCOPYr_chiral_restr0.0570.21399
ELECTRON MICROSCOPYr_gen_planes_refined0.0060.0211232
ELECTRON MICROSCOPYr_gen_planes_other0.0020.022296
ELECTRON MICROSCOPYr_nbd_refined
ELECTRON MICROSCOPYr_nbd_other
ELECTRON MICROSCOPYr_nbtor_refined
ELECTRON MICROSCOPYr_nbtor_other
ELECTRON MICROSCOPYr_xyhbond_nbd_refined
ELECTRON MICROSCOPYr_xyhbond_nbd_other
ELECTRON MICROSCOPYr_metal_ion_refined
ELECTRON MICROSCOPYr_metal_ion_other
ELECTRON MICROSCOPYr_symmetry_vdw_refined
ELECTRON MICROSCOPYr_symmetry_vdw_other
ELECTRON MICROSCOPYr_symmetry_hbond_refined
ELECTRON MICROSCOPYr_symmetry_hbond_other
ELECTRON MICROSCOPYr_symmetry_metal_ion_refined
ELECTRON MICROSCOPYr_symmetry_metal_ion_other
ELECTRON MICROSCOPYr_mcbond_it19.65923.1654604
ELECTRON MICROSCOPYr_mcbond_other19.65723.1654604
ELECTRON MICROSCOPYr_mcangle_it31.9341.7285748
ELECTRON MICROSCOPYr_mcangle_other31.92741.7285749
ELECTRON MICROSCOPYr_scbond_it22.06725.9335061
ELECTRON MICROSCOPYr_scbond_other22.06525.9345062
ELECTRON MICROSCOPYr_scangle_it
ELECTRON MICROSCOPYr_scangle_other36.80346.5367308
ELECTRON MICROSCOPYr_long_range_B_refined65.999268.441319
ELECTRON MICROSCOPYr_long_range_B_other65.999268.441320
ELECTRON MICROSCOPYr_rigid_bond_restr
ELECTRON MICROSCOPYr_sphericity_free
ELECTRON MICROSCOPYr_sphericity_bonded
LS refinement shellResolution: 3→3.078 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0 0 -
Rwork0.621 7997 -
obs--100 %

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