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- EMDB-61211: Human G6PC1 in apo state -

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Basic information

Entry
Database: EMDB / ID: EMD-61211
TitleHuman G6PC1 in apo state
Map data
Sample
  • Complex: Glucose-6-phosphatase catalytic subunit1
    • Protein or peptide: Glucose-6-phosphatase catalytic subunit 1
  • Ligand: (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate
KeywordsG6PC1 / cryo-EM / apo / STRUCTURAL PROTEIN
Function / homology
Function and homology information


glucose-6-phosphatase / Glycogen storage disease type Ia (G6PC) / glucose-6-phosphate transport / glucose-6-phosphatase activity / phosphotransferase activity, alcohol group as acceptor / urate metabolic process / glucose 6-phosphate metabolic process / Gluconeogenesis / glycogen catabolic process / triglyceride metabolic process ...glucose-6-phosphatase / Glycogen storage disease type Ia (G6PC) / glucose-6-phosphate transport / glucose-6-phosphatase activity / phosphotransferase activity, alcohol group as acceptor / urate metabolic process / glucose 6-phosphate metabolic process / Gluconeogenesis / glycogen catabolic process / triglyceride metabolic process / glycogen metabolic process / phosphate ion binding / steroid metabolic process / FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes / cholesterol homeostasis / gluconeogenesis / multicellular organism growth / glucose homeostasis / regulation of gene expression / endoplasmic reticulum membrane / membrane
Similarity search - Function
Glucose-6-phosphatase / Acid phosphatase homologues / Phosphatidic acid phosphatase type 2/haloperoxidase / PAP2 superfamily / Phosphatidic acid phosphatase type 2/haloperoxidase superfamily
Similarity search - Domain/homology
Glucose-6-phosphatase catalytic subunit 1
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.3 Å
AuthorsJiang DH / Xia ZY
Funding support China, 1 items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)31971134 China
CitationJournal: Proc Natl Acad Sci U S A / Year: 2025
Title: Structural insights into glucose-6-phosphate recognition and hydrolysis by human G6PC1.
Authors: Zhanyi Xia / Chuanyu Liu / Di Wu / Huiwen Chen / Jun Zhao / Daohua Jiang /
Abstract: The glucose-6-phosphatase (G6Pase) is an integral membrane protein that catalyzes the hydrolysis of glucose-6-phosphate (G6P) in the endoplasmic reticulum lumen and plays a vital role in glucose ...The glucose-6-phosphatase (G6Pase) is an integral membrane protein that catalyzes the hydrolysis of glucose-6-phosphate (G6P) in the endoplasmic reticulum lumen and plays a vital role in glucose homeostasis. Dysregulation or genetic mutations of G6Pase are associated with diabetes and glycogen storage disease 1a (GSD-1a). Studies have characterized the biophysical and biochemical properties of G6Pase; however, the structure and substrate recognition mechanism of G6Pase remain unclear. Here, we present two cryo-EM structures of the 40-kDa human G6Pase: a wild-type apo form and a mutant G6Pase-H176A with G6P bound, elucidating the structural basis for substrate recognition and hydrolysis. G6Pase comprises nine transmembrane helices and possesses a large catalytic pocket facing the lumen. Unexpectedly, G6P binding induces substantial conformational rearrangements in the catalytic pocket, which facilitate the binding of the sugar moiety. In conjunction with functional analyses, this study provides critical insights into the structure, substrate recognition, catalytic mechanism, and pathology of G6Pase.
History
DepositionAug 19, 2024-
Header (metadata) releaseFeb 5, 2025-
Map releaseFeb 5, 2025-
UpdateFeb 5, 2025-
Current statusFeb 5, 2025Processing site: PDBc / Status: Released

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Structure visualization

Supplemental images

emd_61211.png

Downloads & links

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Map

FileDownload / File: emd_61211.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.85 Å/pix.
x 256 pix.
= 217.6 Å		0.85 Å/pix.
x 256 pix.
= 217.6 Å		0.85 Å/pix.
x 256 pix.
= 217.6 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.85 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.243
Minimum - Maximum-1.2537289 - 1.6474476
Average (Standard dev.)0.000640444 (±0.037728075)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions256256256
Spacing256256256
CellA=B=C: 217.6 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #2

Fileemd_61211_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_61211_half_map_2.map
Projections & Slices
AxesZYX

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Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Glucose-6-phosphatase catalytic subunit1

EntireName: Glucose-6-phosphatase catalytic subunit1
Components
  • Complex: Glucose-6-phosphatase catalytic subunit1
    • Protein or peptide: Glucose-6-phosphatase catalytic subunit 1
  • Ligand: (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate

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Supramolecule #1: Glucose-6-phosphatase catalytic subunit1

SupramoleculeName: Glucose-6-phosphatase catalytic subunit1 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Glucose-6-phosphatase catalytic subunit 1

MacromoleculeName: Glucose-6-phosphatase catalytic subunit 1 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO / EC number: glucose-6-phosphatase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 39.92257 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MEEGMNVLHD FGIQSTHYLQ VNYQDSQDWF ILVSVIADLR NAFYVLFPIW FHLQEAVGIK LLWVAVIGDW LNLVFKWILF GQRPYWWVL DTDYYSNTSV PLIKQFPVTC ETGPGSPSGH AMGTAGVYYV MVTSTLSIFQ GKIKPTYRFR CLNVILWLGF W AVQLNVCL ...String:
MEEGMNVLHD FGIQSTHYLQ VNYQDSQDWF ILVSVIADLR NAFYVLFPIW FHLQEAVGIK LLWVAVIGDW LNLVFKWILF GQRPYWWVL DTDYYSNTSV PLIKQFPVTC ETGPGSPSGH AMGTAGVYYV MVTSTLSIFQ GKIKPTYRFR CLNVILWLGF W AVQLNVCL SRIYLAAHFP HQVVAGVLSG IAVAETFSHI HSIYNASLKK YFLITFFLFS FAIGFYLLLK GLGVDLLWTL EK AQRWCEQ PEWVHIDTTP FASLLKNLGT LFGLGLALNS SMYRESCKGK LSKWLPFRLS SIVASLVLLH VFDSLKPPSQ VEL VFYVLS FCKSAVVPLA SVSVIPYCLA QVLGQP

UniProtKB: Glucose-6-phosphatase catalytic subunit 1

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Macromolecule #2: (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(tri...

MacromoleculeName: (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate
type: ligand / ID: 2 / Number of copies: 8 / Formula: POV
Molecular weightTheoretical: 760.076 Da
Chemical component information

ChemComp-POV:
(2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate / phospholipid*YM

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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: 7.5
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (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: 2.0 µm / Nominal defocus min: 1.0 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: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 102518
Initial angle assignmentType: RANDOM ASSIGNMENT
Final angle assignmentType: MAXIMUM LIKELIHOOD

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