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- PDB-8zvq: Cryo-EM Structure of Human Hormone-sensitive Lipase (HSL) -

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Basic information

Entry
Database: PDB / ID: 8zvq
TitleCryo-EM Structure of Human Hormone-sensitive Lipase (HSL)
ComponentsHormone-sensitive lipase
KeywordsHYDROLASE / Lipid droplets / Lipolysis / Human hormone-sensitive lipase / Hydrolysis of diacylglycerol (DAG)
Function / homology
Function and homology information


hormone-sensitive lipase / diacylglycerol lipase activity / diacylglycerol catabolic process / ether lipid metabolic process / all-trans-retinyl-palmitate hydrolase, all-trans-retinol forming activity / retinyl-palmitate esterase activity / acylglycerol lipase / sterol ester esterase activity / triglyceride catabolic process / monoacylglycerol lipase activity ...hormone-sensitive lipase / diacylglycerol lipase activity / diacylglycerol catabolic process / ether lipid metabolic process / all-trans-retinyl-palmitate hydrolase, all-trans-retinol forming activity / retinyl-palmitate esterase activity / acylglycerol lipase / sterol ester esterase activity / triglyceride catabolic process / monoacylglycerol lipase activity / triacylglycerol lipase activity / Triglyceride catabolism / lipid catabolic process / lipid droplet / cholesterol metabolic process / caveola / MLL4 and MLL3 complexes regulate expression of PPARG target genes in adipogenesis and hepatic steatosis / protein phosphorylation / membrane / cytosol
Similarity search - Function
Hormone-sensitive lipase, N-terminal / Hormone-sensitive lipase (HSL) N-terminus / Lipase, GDXG, putative histidine active site / Lipolytic enzymes "G-D-X-G" family, putative histidine active site. / Lipase, GDXG, putative serine active site / Lipolytic enzymes "G-D-X-G" family, putative serine active site. / Alpha/beta hydrolase fold-3 / alpha/beta hydrolase fold / Alpha/Beta hydrolase fold
Similarity search - Domain/homology
Hormone-sensitive lipase
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.4 Å
AuthorsPeng, H. / Xu, Q. / Wu, J. / Hu, Q.
Funding support1items
OrganizationGrant numberCountry
Not funded
CitationJournal: Nat Commun / Year: 2025
Title: Molecular determinants for the association of human hormone-sensitive lipase with lipid droplets.
Authors: Han Peng / Qikui Xu / Ting Zhang / Jiakai Zhu / Jinheng Pan / Xiaoyu Guan / Shan Feng / Jianping Wu / Qi Hu /
Abstract: Lipid droplets (LDs) are the main cellular storage sites for triacylglycerols (TAGs), playing an important role in energy homeostasis and cell signaling. Hydrolysis of the stored TAGs begins with ...Lipid droplets (LDs) are the main cellular storage sites for triacylglycerols (TAGs), playing an important role in energy homeostasis and cell signaling. Hydrolysis of the stored TAGs begins with conversion of TAGs into diacylglycerols (DAGs) by adipose triglyceride lipase (ATGL), followed by hydrolysis of DAGs by hormone-sensitive lipase (HSL). Despite the central role of HSL in lipolysis, the molecular determinants for its LD association have remained elusive. Here, we report the cryo-EM structure of human HSL at 3.4 Å. Combining this with hydrogen-deuterium exchange mass spectrometry, biochemical and cellular assays, we identify residues 489-538, referred to as the "H-motif", and the N-terminal 4-helix bundle of HSL as LD-binding motifs mediating direct interaction of HSL with LDs. LD binding mediated by the LD-binding motifs is independent of HSL phosphorylation catalyzed by the cAMP-dependent kinase PKA. Our findings provide insight into the LD binding mechanism of HSL, advancing our understanding of the regulation of lipolysis.
History
DepositionJun 11, 2024Deposition site: PDBJ / Processing site: PDBC
Revision 1.0Apr 23, 2025Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Hormone-sensitive lipase
B: Hormone-sensitive lipase


Theoretical massNumber of molelcules
Total (without water)168,4362
Polymers168,4362
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

#1: Protein Hormone-sensitive lipase / HSL / Monoacylglycerol lipase LIPE / Retinyl ester hydrolase / REH


Mass: 84218.227 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: LIPE / Production host: Homo sapiens (human)
References: UniProt: Q05469, hormone-sensitive lipase, acylglycerol lipase
Has protein modificationN

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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: Human Hormone-sensitive Lipase (HSL) / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT
Source (natural)Organism: Homo sapiens (human)
Source (recombinant)Organism: Homo sapiens (human)
Buffer solutionpH: 8
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: 1500 nm
Image recordingElectron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k)

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Processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 384309 / Symmetry type: POINT

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