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- EMDB-42475: PLCb3-Gaq complex on membranes -

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Basic information

Entry
Database: EMDB / ID: EMD-42475
TitlePLCb3-Gaq complex on membranes
Map datafinal sharpened map used for model buidling
Sample
  • Complex: PLCb3-Gaq complex
    • Protein or peptide: Guanine nucleotide-binding protein G(q) subunit alpha
    • Protein or peptide: 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3
  • Ligand: GUANOSINE-5'-DIPHOSPHATE
  • Ligand: TETRAFLUOROALUMINATE ION
  • Ligand: MAGNESIUM ION
  • Ligand: CALCIUM ION
  • Ligand: water
KeywordsPLCb3 / Gaq / SIGNALING PROTEIN
Function / homology
Function and homology information


phosphoinositide phospholipase C / Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion / Acetylcholine regulates insulin secretion / phosphatidylinositol metabolic process / PLC beta mediated events / phospholipase C-activating dopamine receptor signaling pathway / entrainment of circadian clock / regulation of systemic arterial blood pressure / regulation of platelet activation / phospholipase C activity ...phosphoinositide phospholipase C / Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion / Acetylcholine regulates insulin secretion / phosphatidylinositol metabolic process / PLC beta mediated events / phospholipase C-activating dopamine receptor signaling pathway / entrainment of circadian clock / regulation of systemic arterial blood pressure / regulation of platelet activation / phospholipase C activity / phototransduction, visible light / phosphatidylinositol phospholipase C activity / regulation of canonical Wnt signaling pathway / glutamate receptor signaling pathway / postsynaptic cytosol / action potential / Synthesis of IP3 and IP4 in the cytosol / phosphatidylinositol-mediated signaling / photoreceptor outer segment / lipid catabolic process / release of sequestered calcium ion into cytosol / GTPase activator activity / molecular function activator activity / G protein-coupled receptor binding / negative regulation of protein kinase activity / G-protein beta/gamma-subunit complex binding / adenylate cyclase-activating G protein-coupled receptor signaling pathway / G beta:gamma signalling through PLC beta / Presynaptic function of Kainate receptors / Thromboxane signalling through TP receptor / G protein-coupled acetylcholine receptor signaling pathway / G-protein activation / ADP signalling through P2Y purinoceptor 1 / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / blood coagulation / heterotrimeric G-protein complex / Thrombin signalling through proteinase activated receptors (PARs) / Ca2+ pathway / phospholipase C-activating G protein-coupled receptor signaling pathway / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / G alpha (q) signalling events / nuclear membrane / molecular adaptor activity / calmodulin binding / protein stabilization / cadherin binding / G protein-coupled receptor signaling pathway / lysosomal membrane / GTPase activity / calcium ion binding / synapse / GTP binding / Golgi apparatus / protein-containing complex / extracellular exosome / membrane / nucleus / metal ion binding / plasma membrane / cytosol / cytoplasm
Similarity search - Function
Phospholipase C-beta, C-terminal domain / PLC-beta C terminal / PLC-beta, PH domain / Phospholipase C-beta, C-terminal domain superfamily / : / PH domain / Phosphoinositide phospholipase C beta1-4-like EF-hand domain / Phosphatidylinositol-4, 5-bisphosphate phosphodiesterase beta / G-protein alpha subunit, group Q / Phosphoinositide phospholipase C family ...Phospholipase C-beta, C-terminal domain / PLC-beta C terminal / PLC-beta, PH domain / Phospholipase C-beta, C-terminal domain superfamily / : / PH domain / Phosphoinositide phospholipase C beta1-4-like EF-hand domain / Phosphatidylinositol-4, 5-bisphosphate phosphodiesterase beta / G-protein alpha subunit, group Q / 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 / Guanine nucleotide binding protein (G-protein), alpha subunit / G protein alpha subunit, helical insertion / G-protein alpha subunit / G-alpha domain profile. / G protein alpha subunit / EF-hand domain pair / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Guanine nucleotide-binding protein G(q) subunit alpha / 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.4 Å
AuthorsFalzone ME / MacKinnon R
Funding support United States, 2 items
OrganizationGrant numberCountry
Howard Hughes Medical Institute (HHMI) United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM142137 United States
CitationJournal: Proc Natl Acad Sci U S A / Year: 2023
Title: The mechanism of regulation of -catalyzed hydrolysis.
Authors: Maria E Falzone / Roderick MacKinnon /
Abstract: () enzymes cleave phosphatidylinositol 4,5-bisphosphate ( producing and (diacylglycerol). modulates the function of many ion channels, while and regulate intracellular Ca levels and protein ... () enzymes cleave phosphatidylinositol 4,5-bisphosphate ( producing and (diacylglycerol). modulates the function of many ion channels, while and regulate intracellular Ca levels and protein phosphorylation by protein kinase C, respectively. enzymes are under the control of G protein coupled receptor signaling through direct interactions with G proteins and and have been shown to be coincidence detectors for dual stimulation of and -coupled receptors. are aqueous-soluble cytoplasmic enzymes but partition onto the membrane surface to access their lipid substrate, complicating their functional and structural characterization. Using newly developed methods, we recently showed that activates by recruiting it to the membrane. Using these same methods, here we show that increases the catalytic rate constant, , of . Since stimulation of by depends on an autoinhibitory element (the X-Y linker), we propose that produces partial relief of the X-Y linker autoinhibition through an allosteric mechanism. We also determined membrane-bound structures of the and complexes, which show that these G proteins can bind simultaneously and independently of each other to regulate activity. The structures rationalize a finding in the enzyme assay, that costimulation by both G proteins follows a product rule of each independent stimulus. We conclude that baseline activity of is strongly suppressed, but the effect of G proteins, especially acting together, provides a robust stimulus upon G protein stimulation.
History
DepositionOct 24, 2023-
Header (metadata) releaseDec 6, 2023-
Map releaseDec 6, 2023-
UpdateDec 6, 2023-
Current statusDec 6, 2023Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_42475.png

Downloads & links

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Map

FileDownload / File: emd_42475.map.gz / Format: CCP4 / Size: 155.3 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotationfinal sharpened map used for model buidling
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.84 Å/pix.
x 344 pix.
= 288.616 Å		0.84 Å/pix.
x 344 pix.
= 288.616 Å		0.84 Å/pix.
x 344 pix.
= 288.616 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.839 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.258
Minimum - Maximum-1.9595518 - 3.04214
Average (Standard dev.)-0.00080670335 (±0.06902913)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions344344344
Spacing344344344
CellA=B=C: 288.616 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_42475_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Additional map: final unsharpened map used to assist model building

Fileemd_42475_additional_1.map
Annotationfinal unsharpened map used to assist model building
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #2

Fileemd_42475_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_42475_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : PLCb3-Gaq complex

EntireName: PLCb3-Gaq complex
Components
  • Complex: PLCb3-Gaq complex
    • Protein or peptide: Guanine nucleotide-binding protein G(q) subunit alpha
    • Protein or peptide: 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3
  • Ligand: GUANOSINE-5'-DIPHOSPHATE
  • Ligand: TETRAFLUOROALUMINATE ION
  • Ligand: MAGNESIUM ION
  • Ligand: CALCIUM ION
  • Ligand: water

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Supramolecule #1: PLCb3-Gaq complex

SupramoleculeName: PLCb3-Gaq complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Guanine nucleotide-binding protein G(q) subunit alpha

MacromoleculeName: Guanine nucleotide-binding protein G(q) subunit alpha / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 41.676387 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: GPMACCLSEE AKEARRINDE IERQLRRDKR DARRELKLLL LGTGESGKST FIKQMRIIHG SGYSDEDKRG FTKLVYQNIF TAMQAMIRA MDTLKIPYKY EHNKAHAQLV REVDVEKVSA FENPYVDAIK SLWNDPGIQE CYDRRREYQL SDSTKYYLND L DRVADPAY ...String:
GPMACCLSEE AKEARRINDE IERQLRRDKR DARRELKLLL LGTGESGKST FIKQMRIIHG SGYSDEDKRG FTKLVYQNIF TAMQAMIRA MDTLKIPYKY EHNKAHAQLV REVDVEKVSA FENPYVDAIK SLWNDPGIQE CYDRRREYQL SDSTKYYLND L DRVADPAY LPTQQDVLRV RVPTTGIIEY PFDLQSVIFR MVDVGGQRSE RRKWIHCFEN VTSIMFLVAL SEYDQVLVES DN ENRMEES KALFRTIITY PWFQNSSVIL FLNKKDLLEE KIMYSHLVDY FPEYDGPQRD AQAAREFILK MFVDLNPDSD KII YSHFTC ATDTENIRFV FAAVKDTILQ LNLKEYNLV

UniProtKB: Guanine nucleotide-binding protein G(q) subunit alpha

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Macromolecule #2: 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3

MacromoleculeName: 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3
type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO / EC number: phosphoinositide phospholipase C
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 139.104719 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: GPAMDPEFMA LQLEPPTVVE TLRRGSKFIK WDEETSSRNL VTLRVDPNGF FLYWTGPNME VDTLDISSIR DTRTGRYARL PKDPKIREV LGFGGPDARL EEKLMTVVSG PDPVNTVFLN FMAVQDDTAK VWSEELFKLA MNILAQNASR NTFLRKAYTK L KLQVNQDG ...String:
GPAMDPEFMA LQLEPPTVVE TLRRGSKFIK WDEETSSRNL VTLRVDPNGF FLYWTGPNME VDTLDISSIR DTRTGRYARL PKDPKIREV LGFGGPDARL EEKLMTVVSG PDPVNTVFLN FMAVQDDTAK VWSEELFKLA MNILAQNASR NTFLRKAYTK L KLQVNQDG RIPVKNILKM FSADKKRVET ALESCGLKFN RSESIRPDEF SLEIFERFLN KLCLRPDIDK ILLEIGAKGK PY LTLEQLM DFINQKQRDP RLNEVLYPPL RPSQARLLIE KYEPNQQFLE RDQMSMEGFS RYLGGEENGI LPLEALDLST DMT QPLSAY FINSSHNTYL TAGQLAGTSS VEMYRQALLW GCRCVELDVW KGRPPEEEPF ITHGFTMTTE VPLRDVLEAI AETA FKTSP YPVILSFENH VDSAKQQAKM AEYCRSIFGD ALLIEPLDKY PLAPGVPLPS PQDLMGRILV KNKKRHRPSA GGPDS AGRK RPLEQSNSAL SESSAATEPS SPQLGSPSSD SCPGLSNGEE VGLEKPSLEP QKSLGDEGLN RGPYVLGPAD REDEEE DEE EEEQTDPKKP TTDEGTASSE VNATEEMSTL VNYIEPVKFK SFEAARKRNK CFEMSSFVET KAMEQLTKSP MEFVEYN KQ QLSRIYPKGT RVDSSNYMPQ LFWNVGCQLV ALNFQTLDVA MQLNAGVFEY NGRSGYLLKP EFMRRPDKSF DPFTEVIV D GIVANALRVK VISGQFLSDR KVGIYVEVDM FGLPVDTRRK YRTRTSQGNS FNPVWDEEPF DFPKVVLPTL ASLRIAAFE EGGKFVGHRI LPVSAIRSGY HYVCLRNEAN QPLCLPALLI YTEASDYIPD DHQDYAEALI NPIKHVSLMD QRARQLAALI GESEAQAGQ ETCQDTQSQQ LGSQPSSNPT PSPLDASPRR PPGPTTSPAS TSLSSPGQRD DLIASILSEV APTPLDELRG H KALVKLRS RQERDLRELR KKHQRKAVTL TRRLLDGLAQ AQAEGRCRLR PGALGGAADV EDTKEGEDEA KRYQEFQNRQ VQ SLLELRE AQVDAEAQRR LEHLRQALQR LREVVLDANT TQFKRLKEMN EREKKELQKI LDRKRHNSIS EAKMRDKHKK EAE LTEINR RHITESVNSI RRLEEAQKQR HDRLVAGQQQ VLQQLAEEEP KLLAQLAQEC QEQRARLPQE IRRSLLGEMP EGLG DGPLV ACASNGHAPG SSGHLSGADS ESQEENTQL

UniProtKB: 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3

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Macromolecule #3: GUANOSINE-5'-DIPHOSPHATE

MacromoleculeName: GUANOSINE-5'-DIPHOSPHATE / type: ligand / ID: 3 / Number of copies: 1 / Formula: GDP
Molecular weightTheoretical: 443.201 Da
Chemical component information

ChemComp-GDP:
GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying molecule*YM

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Macromolecule #4: TETRAFLUOROALUMINATE ION

MacromoleculeName: TETRAFLUOROALUMINATE ION / type: ligand / ID: 4 / Number of copies: 1 / Formula: ALF
Molecular weightTheoretical: 102.975 Da
Chemical component information

ChemComp-ALF:
TETRAFLUOROALUMINATE ION

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Macromolecule #5: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 5 / Number of copies: 1 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Macromolecule #6: CALCIUM ION

MacromoleculeName: CALCIUM ION / type: ligand / ID: 6 / Number of copies: 1 / Formula: CA
Molecular weightTheoretical: 40.078 Da

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Macromolecule #7: water

MacromoleculeName: water / type: ligand / ID: 7 / Number of copies: 1 / Formula: HOH
Molecular weightTheoretical: 18.015 Da
Chemical component information

ChemComp-HOH:
WATER

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.4
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 60.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.5 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 67545
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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