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- EMDB-60512: Cryo-EM Structure of Human Hormone-sensitive Lipase (HSL) -

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Basic information

Entry
Database: EMDB / ID: EMD-60512
TitleCryo-EM Structure of Human Hormone-sensitive Lipase (HSL)
Map data
Sample
  • Complex: Human Hormone-sensitive Lipase (HSL)
    • Protein or peptide: Hormone-sensitive lipase
KeywordsLipid droplets / Lipolysis / Human hormone-sensitive lipase / Hydrolysis of diacylglycerol (DAG) / HYDROLASE
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)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.4 Å
AuthorsPeng H / Xu Q / Wu J / Hu Q
Funding support1 items
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, 2024-
Header (metadata) releaseApr 23, 2025-
Map releaseApr 23, 2025-
UpdateApr 23, 2025-
Current statusApr 23, 2025Processing site: PDBc / Status: Released

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Structure visualization

Supplemental images

emd_60512.png

Downloads & links

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Map

FileDownload / File: emd_60512.map.gz / Format: CCP4 / Size: 38.4 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

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AxesZ (Sec.)Y (Row.)X (Col.)
1.09 Å/pix.
x 216 pix.
= 234.792 Å		1.09 Å/pix.
x 216 pix.
= 234.792 Å		1.09 Å/pix.
x 216 pix.
= 234.792 Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.087 Å
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Histogram (log scale)
Contour LevelBy AUTHOR: 0.5
Minimum - Maximum-4.6737685 - 7.1335955
Average (Standard dev.)0.0006413931 (±0.14510415)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions216216216
Spacing216216216
CellA=B=C: 234.792 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_60512_msk_1.map
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Half map: #2

Fileemd_60512_half_map_1.map
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Half map: #1

Fileemd_60512_half_map_2.map
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Sample components

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Entire : Human Hormone-sensitive Lipase (HSL)

EntireName: Human Hormone-sensitive Lipase (HSL)
Components
  • Complex: Human Hormone-sensitive Lipase (HSL)
    • Protein or peptide: Hormone-sensitive lipase

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Supramolecule #1: Human Hormone-sensitive Lipase (HSL)

SupramoleculeName: Human Hormone-sensitive Lipase (HSL) / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Hormone-sensitive lipase

MacromoleculeName: Hormone-sensitive lipase / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO / EC number: hormone-sensitive lipase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 84.218227 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MDLRTMTQSL VTLAEDNIAF FSSQGPGETA QRLSGVFAGV REQALGLEPA LGRLLGVAHL FDLDPETPAN GYRSLVHTAR CCLAHLLHK SRYVASNRRS IFFRTSHNLA ELEAYLAALT QLRALVYYAQ RLLVTNRPGV LFFEGDEGLT ADFLREYVTL H KGCFYGRC ...String:
MDLRTMTQSL VTLAEDNIAF FSSQGPGETA QRLSGVFAGV REQALGLEPA LGRLLGVAHL FDLDPETPAN GYRSLVHTAR CCLAHLLHK SRYVASNRRS IFFRTSHNLA ELEAYLAALT QLRALVYYAQ RLLVTNRPGV LFFEGDEGLT ADFLREYVTL H KGCFYGRC LGFQFTPAIR PFLQTISIGL VSFGEHYKRN ETGLSVAASS LFTSGRFAID PELRGAEFER ITQNLDVHFW KA FWNITEM EVLSSLANMA SATVRVSRLL SLPPEAFEMP LTADPTLTVT ISPPLAHTGP GPVLVRLISY DLREGQDSEE LSS LIKSNG QRSLELWPRP QQAPRSRSLI VHFHGGGFVA QTSRSHEPYL KSWAQELGAP IISIDYSLAP EAPFPRALEE CFFA YCWAI KHCALLGSTG ERICLAGDSA GGNLCFTVAL RAAAYGVRVP DGIMAAYPAT MLQPAASPSR LLSLMDPLLP LSVLS KCVS AYAGAKTEDH SNSDQKALGM MGLVRRDTAL LLRDFRLGAS SWLNSFLELS GRKSQKMSEP IAEPMRRSVS EAALAQ PQG PLGTDSLKNL TLRDLSLRGN SETSSDTPEM SLSAETLSPS TPSDVNFLLP PEDAGEEAEA KNELSPMDRG LGVRAAF PE GFHPRRSSQG ATQMPLYSSP IVKNPFMSPL LAPDSMLKSL PPVHIVACAL DPMLDDSVML ARRLRNLGQP VTLRVVED L PHGFLTLAAL CRETRQAAEL CVERIRLVLT PPAGAGPSGE TGAAGVDGGC GGRH

UniProtKB: Hormone-sensitive lipase

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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: 8
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 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: 1.5 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 384309
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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