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- PDB-9j7u: H176A mutant of human G6PC1 in complex with G6P -

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Basic information

Entry
Database: PDB / ID: 9j7u
TitleH176A mutant of human G6PC1 in complex with G6P
ComponentsGlucose-6-phosphatase catalytic subunit 1
KeywordsSTRUCTURAL PROTEIN / G6PC1 / cryo-EM / G6P
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
6-O-phosphono-beta-D-glucopyranose / Chem-POV / Glucose-6-phosphatase catalytic subunit 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.14 Å
AuthorsJiang, D.H. / Xia, Z.Y.
Funding support China, 1items
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, 2024Deposition site: PDBJ / Processing site: PDBC
Revision 1.0Feb 5, 2025Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Glucose-6-phosphatase catalytic subunit 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)42,3965
Polymers39,8561
Non-polymers2,5404
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 Glucose-6-phosphatase catalytic subunit 1 / Glucose-6-phosphatase / G-6-Pase / G6Pase / Glucose-6-phosphatase alpha / G6Pase-alpha


Mass: 39855.504 Da / Num. of mol.: 1 / Mutation: H176A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: G6PC1, G6PC, G6PT / Production host: Homo sapiens (human) / References: UniProt: P35575, glucose-6-phosphatase
#2: Sugar ChemComp-BG6 / 6-O-phosphono-beta-D-glucopyranose / BETA-D-GLUCOSE-6-PHOSPHATE / 6-O-phosphono-beta-D-glucose / 6-O-phosphono-D-glucose / 6-O-phosphono-glucose


Type: D-saccharide, beta linking / Mass: 260.136 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C6H13O9P / Feature type: SUBJECT OF INVESTIGATION
IdentifierTypeProgram
b-D-Glcp6PO3IUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
#3: Chemical ChemComp-POV / (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate / POPC


Mass: 760.076 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C42H82NO8P / Feature type: SUBJECT OF INVESTIGATION / Comment: phospholipid*YM
Has ligand of interestY
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: Glucose-6-phosphatase catalytic subunit1 / Type: COMPLEX / Entity ID: #1 / Source: RECOMBINANT
Source (natural)Organism: Homo sapiens (human)
Source (recombinant)Organism: Homo sapiens (human)
Buffer solutionpH: 7.5
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: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 1000 nm
Image recordingElectron dose: 60 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: 3.14 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 170633 / Symmetry type: POINT
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.0032977
ELECTRON MICROSCOPYf_angle_d0.5134056
ELECTRON MICROSCOPYf_dihedral_angle_d5.971406
ELECTRON MICROSCOPYf_chiral_restr0.039456
ELECTRON MICROSCOPYf_plane_restr0.006487

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