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- PDB-7zeu: Crystal structure of human Clusterin, crystal form II -

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Basic information

Entry
Database: PDB / ID: 7zeu
TitleCrystal structure of human Clusterin, crystal form II
ComponentsClusterin
KeywordsCHAPERONE / molecular chaperone / complement system / Alzheimer's disease
Function / homology
Function and homology information


immune complex clearance / perinuclear endoplasmic reticulum lumen / regulation of neuronal signal transduction / positive regulation of neurofibrillary tangle assembly / central nervous system myelin maintenance / response to misfolded protein / negative regulation of response to endoplasmic reticulum stress / spherical high-density lipoprotein particle / Terminal pathway of complement / protein targeting to lysosome involved in chaperone-mediated autophagy ...immune complex clearance / perinuclear endoplasmic reticulum lumen / regulation of neuronal signal transduction / positive regulation of neurofibrillary tangle assembly / central nervous system myelin maintenance / response to misfolded protein / negative regulation of response to endoplasmic reticulum stress / spherical high-density lipoprotein particle / Terminal pathway of complement / protein targeting to lysosome involved in chaperone-mediated autophagy / protein carrier chaperone / chromaffin granule / regulation of amyloid-beta clearance / microglial cell proliferation / reverse cholesterol transport / misfolded protein binding / negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage / apical dendrite / protein import / complement activation / positive regulation of ubiquitin-dependent protein catabolic process / negative regulation of amyloid fibril formation / Antimicrobial peptides / low-density lipoprotein particle receptor binding / neurofibrillary tangle / positive regulation of amyloid fibril formation / positive regulation of amyloid-beta formation / negative regulation of release of cytochrome c from mitochondria / amyloid-beta clearance / negative regulation of amyloid-beta formation / complement activation, classical pathway / chaperone-mediated protein complex assembly / negative regulation of protein-containing complex assembly / positive regulation of intrinsic apoptotic signaling pathway / : / intrinsic apoptotic signaling pathway / platelet alpha granule lumen / Regulation of Complement cascade / release of cytochrome c from mitochondria / positive regulation of protein-containing complex assembly / microglial cell activation / positive regulation of NF-kappaB transcription factor activity / positive regulation of receptor-mediated endocytosis / lipid metabolic process / tau protein binding / response to virus / cell morphogenesis / positive regulation of nitric oxide biosynthetic process / positive regulation of tumor necrosis factor production / unfolded protein binding / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / Platelet degranulation / regulation of cell population proliferation / protein-folding chaperone binding / : / amyloid-beta binding / blood microparticle / regulation of apoptotic process / negative regulation of neuron apoptotic process / mitochondrial inner membrane / protein stabilization / positive regulation of apoptotic process / receptor ligand activity / signaling receptor binding / innate immune response / intracellular membrane-bounded organelle / ubiquitin protein ligase binding / synapse / positive regulation of gene expression / protein-containing complex binding / perinuclear region of cytoplasm / cell surface / Golgi apparatus / protein-containing complex / mitochondrion / extracellular space / extracellular exosome / extracellular region / nucleus / cytosol / cytoplasm
Similarity search - Function
Clusterin-like / Clusterin, N-terminal / Clusterin, C-terminal / Clusterin / Clusterin, conserved site / Clusterin / Clusterin signature 1. / Clusterin signature 2. / CLUSTERIN Beta chain / CLUSTERIN alpha chain
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 3.5 Å
AuthorsYuste-Checa, P. / Bracher, A. / Hartl, F.U.
Funding support1items
OrganizationGrant numberCountry
Not funded
Citation
Journal: Nat.Struct.Mol.Biol. / Year: 2025
Title: Structural analyses define the molecular basis of clusterin chaperone function.
Authors: Yuste-Checa, P. / Carvajal, A.I. / Mi, C. / Paatz, S. / Hartl, F.U. / Bracher, A.
#1: Journal: Biorxiv / Year: 2024
Title: Hydrophobic tails enable diverse functions of the extracellular chaperone clusterin
Authors: Yuste-Checa, P. / Carvajal, A.I. / Mi, C. / Paatz, S. / Ulrich Hartl, F. / Bracher, A.
History
DepositionMar 31, 2022Deposition site: PDBE / Processing site: PDBE
Revision 1.0Oct 11, 2023Provider: repository / Type: Initial release
Revision 1.1Nov 6, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature / Item: _pdbx_entry_details.has_protein_modification
Revision 1.2Apr 23, 2025Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.title / _citation.year
Revision 1.3Sep 17, 2025Group: Database references / Category: citation / citation_author

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Clusterin
D: Clusterin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)97,74814
Polymers94,0782
Non-polymers3,67012
Water00
1
A: Clusterin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)48,5697
Polymers47,0391
Non-polymers1,5306
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
D: Clusterin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)49,1797
Polymers47,0391
Non-polymers2,1406
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)194.440, 46.438, 155.173
Angle α, β, γ (deg.)90.000, 127.200, 90.000
Int Tables number5
Space group name H-MC121

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Components

#1: Protein Clusterin / Aging-associated gene 4 protein / Apolipoprotein J / Apo-J / Complement cytolysis inhibitor / CLI / ...Aging-associated gene 4 protein / Apolipoprotein J / Apo-J / Complement cytolysis inhibitor / CLI / Complement-associated protein SP-40 / 40 / Ku70-binding protein 1 / NA1/NA2 / Sulfated glycoprotein 2 / SGP-2 / Testosterone-repressed prostate message 2 / TRPM-2


Mass: 47038.852 Da / Num. of mol.: 2 / Fragment: Clu-delta(214-238) / Mutation: deletion(214-238)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CLU, APOJ, CLI, KUB1, AAG4 / Plasmid: pB-T-PAF / Cell line (production host): HEK293T / Production host: Homo sapiens (human) / References: UniProt: P10909
#2: Polysaccharide
2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 424.401 Da / Num. of mol.: 5
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAcb1-4DGlcpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}LINUCSPDB-CARE
#3: Sugar
ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0
Has ligand of interestN
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.97 Å3/Da / Density % sol: 58.53 % / Mosaicity: 0.29 °
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop / pH: 5 / Details: 24% PEG-1500, 20% glycerol

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID23-1 / Wavelength: 0.7749 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Dec 2, 2021
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.7749 Å / Relative weight: 1
ReflectionResolution: 3.5→48.59 Å / Num. obs: 14413 / % possible obs: 99.8 % / Redundancy: 7.2 % / Biso Wilson estimate: 108.57 Å2 / CC1/2: 0.995 / Rmerge(I) obs: 0.211 / Rpim(I) all: 0.085 / Rrim(I) all: 0.229 / Net I/σ(I): 6.1 / Num. measured all: 103733 / Scaling rejects: 23
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. measured allNum. unique obsCC1/2Rpim(I) allRrim(I) allNet I/σ(I) obs% possible all
3.5-3.835.71.5171944934080.6190.6721.6641.499.6
8.57-48.596.80.077713010530.9950.0310.08319.399.4

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Phasing

PhasingMethod: molecular replacement
Phasing MRR rigid body: 0.582
Highest resolutionLowest resolution
Rotation77.69 Å3.5 Å

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Processing

Software
NameVersionClassification
XDSVERSION Feb 5, 2021data reduction
Aimless0.7.4data scaling
MOLREP11.4.06phasing
PHENIX1.19.2-4158refinement
PDB_EXTRACT3.27data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 7ZET

7zet


Resolution: 3.5→29.77 Å / SU ML: 0.5 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 35.05 / Stereochemistry target values: ML
Details: The Clusterin construct is a glyco-protein, which was expressed in the presence of the alpha-mannosidase I inhibitor kifunensine. Kifunensine prevents trimming of mannose moieties, resulting ...Details: The Clusterin construct is a glyco-protein, which was expressed in the presence of the alpha-mannosidase I inhibitor kifunensine. Kifunensine prevents trimming of mannose moieties, resulting in oligo-mannose N-glycans, and thereby prevents processing to mature complex N-glycans (Chang et al., Structure 15, 267(2007), Fig. 1B). Asn residues 86, 103, 145, 291, 354 and 374 are expected to carry predominantly NAG-NAG-BMA-(3->1)MAN-MAN-MAN (6->1)-MAN (3->1)MAN-MAN (6->1)MAN-MAN N-glycan trees (Chang et al., Structure 15, 267(2007), Fig. 1B).
RfactorNum. reflection% reflection
Rfree0.2836 692 4.83 %
Rwork0.2352 13639 -
obs0.2375 14331 99.65 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 264.62 Å2 / Biso mean: 137.2869 Å2 / Biso min: 53.43 Å2
Refinement stepCycle: final / Resolution: 3.5→29.77 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5726 0 238 0 5964
Biso mean--182.16 --
Num. residues----724
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 5

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
3.5-3.770.37951560.32032665282199
3.77-4.150.3371560.259526832839100
4.15-4.750.29871310.21762710284199
4.75-5.970.26711360.246227322868100
5.97-29.770.23321130.210428492962100

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