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- PDB-1nfo: APOLIPOPROTEIN E2 (APOE2, D154A MUTATION) -

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Basic information

Entry
Database: PDB / ID: 1nfo
TitleAPOLIPOPROTEIN E2 (APOE2, D154A MUTATION)
ComponentsAPOLIPOPROTEIN E2
KeywordsLIPID TRANSPORT / HEPARIN-BINDING / PLASMA PROTEIN / HDL / VLDL
Function / homology
Function and homology information


lipid transport involved in lipid storage / intermediate-density lipoprotein particle clearance / positive regulation of lipid transport across blood-brain barrier / regulation of cellular response to very-low-density lipoprotein particle stimulus / metal chelating activity / triglyceride-rich lipoprotein particle clearance / discoidal high-density lipoprotein particle / lipoprotein particle / negative regulation of triglyceride metabolic process / maintenance of location in cell ...lipid transport involved in lipid storage / intermediate-density lipoprotein particle clearance / positive regulation of lipid transport across blood-brain barrier / regulation of cellular response to very-low-density lipoprotein particle stimulus / metal chelating activity / triglyceride-rich lipoprotein particle clearance / discoidal high-density lipoprotein particle / lipoprotein particle / negative regulation of triglyceride metabolic process / maintenance of location in cell / regulation of amyloid-beta clearance / negative regulation of cholesterol biosynthetic process / positive regulation of lipoprotein transport / Transcriptional regulation by the AP-2 (TFAP2) family of transcription factors / chylomicron remnant clearance / chylomicron remnant / intermediate-density lipoprotein particle / acylglycerol homeostasis / NMDA glutamate receptor clustering / very-low-density lipoprotein particle remodeling / Chylomicron clearance / phosphatidylcholine-sterol O-acyltransferase activator activity / positive regulation of phospholipid efflux / Chylomicron remodeling / positive regulation of low-density lipoprotein particle receptor catabolic process / response to caloric restriction / cellular response to lipoprotein particle stimulus / lipid transporter activity / very-low-density lipoprotein particle clearance / Chylomicron assembly / high-density lipoprotein particle clearance / phospholipid efflux / chylomicron / regulation of protein metabolic process / very-low-density lipoprotein particle receptor binding / regulation of amyloid fibril formation / lipoprotein catabolic process / AMPA glutamate receptor clustering / high-density lipoprotein particle remodeling / melanosome organization / positive regulation of cholesterol metabolic process / multivesicular body, internal vesicle / regulation of behavioral fear response / reverse cholesterol transport / positive regulation of amyloid-beta clearance / high-density lipoprotein particle assembly / low-density lipoprotein particle / host-mediated activation of viral process / lipoprotein biosynthetic process / cholesterol transfer activity / high-density lipoprotein particle / protein import / very-low-density lipoprotein particle / cholesterol catabolic process / heparan sulfate proteoglycan binding / low-density lipoprotein particle remodeling / amyloid precursor protein metabolic process / negative regulation of amyloid fibril formation / regulation of Cdc42 protein signal transduction / positive regulation of membrane protein ectodomain proteolysis / synaptic transmission, cholinergic / regulation of amyloid precursor protein catabolic process / HDL remodeling / negative regulation of endothelial cell migration / cholesterol efflux / regulation of cholesterol metabolic process / artery morphogenesis / regulation of axon extension / negative regulation of protein metabolic process / Scavenging by Class A Receptors / triglyceride homeostasis / triglyceride metabolic process / low-density lipoprotein particle receptor binding / positive regulation of amyloid fibril formation / regulation of innate immune response / virion assembly / positive regulation of dendritic spine development / negative regulation of endothelial cell proliferation / response to dietary excess / antioxidant activity / negative regulation of MAP kinase activity / negative regulation of amyloid-beta formation / lipoprotein particle binding / locomotory exploration behavior / negative regulation of long-term synaptic potentiation / positive regulation of endocytosis / negative regulation of blood vessel endothelial cell migration / negative regulation of platelet activation / negative regulation of blood coagulation / positive regulation of dendritic spine maintenance / regulation of neuronal synaptic plasticity / positive regulation of cholesterol efflux / negative regulation of protein secretion / fatty acid homeostasis / long-term memory / regulation of protein-containing complex assembly / synaptic cleft / long-chain fatty acid transport / intracellular transport / positive regulation of lipid biosynthetic process
Similarity search - Function
Apolipoprotein / Apolipoprotein A/E / : / Apolipoprotein A1/A4/E domain / Four Helix Bundle (Hemerythrin (Met), subunit A) / Up-down Bundle / Mainly Alpha
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2 Å
AuthorsRupp, B. / Parkin, S.
CitationJournal: Nat.Struct.Biol. / Year: 1996
Title: Novel mechanism for defective receptor binding of apolipoprotein E2 in type III hyperlipoproteinemia.
Authors: Dong, L.M. / Parkin, S. / Trakhanov, S.D. / Rupp, B. / Simmons, T. / Arnold, K.S. / Newhouse, Y.M. / Innerarity, T.L. / Weisgraber, K.H.
History
DepositionJul 17, 1996Processing site: BNL
Revision 1.0Jan 27, 1997Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Nov 3, 2021Group: Database references / Category: database_2 / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details
Revision 1.4Aug 9, 2023Group: Refinement description / Category: pdbx_initial_refinement_model
Revision 1.5May 22, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: APOLIPOPROTEIN E2


Theoretical massNumber of molelcules
Total (without water)22,0641
Polymers22,0641
Non-polymers00
Water2,540141
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)40.613, 53.671, 84.795
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein APOLIPOPROTEIN E2 / APOE2


Mass: 22064.021 Da / Num. of mol.: 1 / Fragment: 22KD RECEPTOR BINDING DOMAIN / Mutation: D154A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: E2 / Organ: PLASMA / Production host: Escherichia coli (E. coli) / References: UniProt: P02649
#2: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 141 / Source method: isolated from a natural source / Formula: H2O

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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: 3.07 Å3/Da / Density % sol: 59.9 %
Crystal grow
*PLUS
Method: vapor diffusion, hanging drop / Details: Wilson, C., (1991) Science, 252, 1817. / PH range low: 5.3 / PH range high: 4.5
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-ID
110 mg/mlprotein1drop
215 %PEG4001drop
320 mMsodium acetate1drop
40.2 %beta-n-octylglucopyranoside1drop
50.1 %beta-mercaptoethanol1drop

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Data collection

DiffractionMean temperature: 130 K
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU RUH2R / Wavelength: 1.5418
DetectorType: ADSC / Detector: AREA DETECTOR
RadiationMonochromator: GRAPHITE(002) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 2→15 Å / % possible obs: 94.2 % / Redundancy: 3.5 % / Rmerge(I) obs: 0.0509
Reflection
*PLUS
Num. obs: 8964 / Observed criterion σ(I): 2

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Processing

Software
NameClassification
SHELXL-93model building
X-PLORmodel building
SHELXL-93refinement
X-PLORrefinement
ADSCdata collection
SHELXL-93phasing
X-PLORphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PHASING MODEL DERIVED FROM 1NFN

1nfn


Resolution: 2→8 Å / Num. parameters: 5267 / Num. restraintsaints: 4789 / Cross valid method: R-FREE / σ(F): 0
Details: RESIDUES 23 AND 24 ARE NOT WELL DEFINED AND THE BOND ANGLES ARE ON THE BORDERLINE OF THE ALLOWED REGIONS. CONSIDERING THE WEAK ELECTRON DENSITY THERE IS NO POINT IN ATTEMPTING TO ACCURATELY ...Details: RESIDUES 23 AND 24 ARE NOT WELL DEFINED AND THE BOND ANGLES ARE ON THE BORDERLINE OF THE ALLOWED REGIONS. CONSIDERING THE WEAK ELECTRON DENSITY THERE IS NO POINT IN ATTEMPTING TO ACCURATELY REFINE THESE TWO RESIDUES.
RfactorNum. reflection% reflectionSelection details
Rfree0.27 1248 10 %EVERY 10TH REFLECTION
all0.221 12485 --
obs0.206 -94.2 %-
Solvent computationSolvent model: 'SWAT' IN SHELXL93
Refinement stepCycle: LAST / Resolution: 2→8 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1075 0 0 143 1218
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONs_bond_d0.01
X-RAY DIFFRACTIONs_angle_d2
X-RAY DIFFRACTIONs_similar_dist
X-RAY DIFFRACTIONs_from_restr_planes0.103
X-RAY DIFFRACTIONs_zero_chiral_vol0.06
X-RAY DIFFRACTIONs_non_zero_chiral_vol
X-RAY DIFFRACTIONs_anti_bump_dis_restr0.052
X-RAY DIFFRACTIONs_rigid_bond_adp_cmpnt
X-RAY DIFFRACTIONs_similar_adp_cmpnt0.038
X-RAY DIFFRACTIONs_approx_iso_adps0.047
Software
*PLUS
Name: SHELXL-93 / Classification: refinement
Refinement
*PLUS
Rfactor Rfree: 0.27
Solvent computation
*PLUS
Displacement parameters
*PLUS

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