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- PDB-4ddp: crystal structure of Beclin 1 evolutionarily conserved domain(ECD) -

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Basic information

Entry
Database: PDB / ID: 4ddp
Titlecrystal structure of Beclin 1 evolutionarily conserved domain(ECD)
ComponentsBeclin-1
KeywordsMEMBRANE PROTEIN / Beclin 1 / ECD / autophagy / membrane binding
Function / homology
Function and homology information


cellular response to aluminum ion / phosphatidylinositol 3-kinase complex, class III / phosphatidylinositol 3-kinase complex, class III, type II / positive regulation of stress granule assembly / cellular response to oxygen-glucose deprivation / phosphatidylinositol 3-kinase complex, class III, type I / response to mitochondrial depolarisation / positive regulation of attachment of mitotic spindle microtubules to kinetochore / cytoplasmic side of mitochondrial outer membrane / negative regulation of lysosome organization ...cellular response to aluminum ion / phosphatidylinositol 3-kinase complex, class III / phosphatidylinositol 3-kinase complex, class III, type II / positive regulation of stress granule assembly / cellular response to oxygen-glucose deprivation / phosphatidylinositol 3-kinase complex, class III, type I / response to mitochondrial depolarisation / positive regulation of attachment of mitotic spindle microtubules to kinetochore / cytoplasmic side of mitochondrial outer membrane / negative regulation of lysosome organization / positive regulation of autophagosome assembly / negative regulation of autophagosome assembly / receptor catabolic process / engulfment of apoptotic cell / suppression by virus of host autophagy / protein targeting to lysosome / early endosome to late endosome transport / late endosome to vacuole transport / cellular response to nitrogen starvation / SMAD protein signal transduction / Translation of Replicase and Assembly of the Replication Transcription Complex / phagophore assembly site / negative regulation of programmed cell death / response to iron(II) ion / phosphatidylinositol-3-phosphate biosynthetic process / mitotic metaphase chromosome alignment / cytoplasmic pattern recognition receptor signaling pathway / Macroautophagy / RSV-host interactions / lysosome organization / positive regulation of cardiac muscle hypertrophy / p38MAPK cascade / mitophagy / autophagosome maturation / autophagosome assembly / negative regulation of reactive oxygen species metabolic process / neuron development / autophagosome / response to vitamin E / regulation of macroautophagy / amyloid-beta metabolic process / cellular defense response / cellular response to glucose starvation / positive regulation of autophagy / phosphatidylinositol 3-kinase binding / positive regulation of intrinsic apoptotic signaling pathway / JNK cascade / cellular response to epidermal growth factor stimulus / cellular response to copper ion / cellular response to amino acid starvation / phagocytic vesicle / regulation of cytokinesis / regulation of autophagy / macroautophagy / Antigen Presentation: Folding, assembly and peptide loading of class I MHC / response to lead ion / trans-Golgi network / ISG15 antiviral mechanism / autophagy / cellular response to hydrogen peroxide / GTPase binding / protein-macromolecule adaptor activity / Translation of Replicase and Assembly of the Replication Transcription Complex / protein-containing complex assembly / defense response to virus / molecular adaptor activity / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / nuclear body / endosome membrane / response to hypoxia / Ub-specific processing proteases / endosome / response to xenobiotic stimulus / negative regulation of cell population proliferation / cell division / apoptotic process / ubiquitin protein ligase binding / dendrite / endoplasmic reticulum membrane / negative regulation of apoptotic process / protein kinase binding / SARS-CoV-2 activates/modulates innate and adaptive immune responses / endoplasmic reticulum / identical protein binding / cytoplasm / cytosol
Similarity search - Function
Autophagy protein 6/Beclin 1 / Beclin-1, BH3 domain / Beclin-1 BH3 domain, Bcl-2-interacting / Atg6/Beclin / Atg6/Beclin C-terminal domain superfamily / Atg6, BARA domain / Atg6/beclin, coiled-coil domain / Apg6 BARA domain / Apg6 coiled-coil region / Actin-binding Protein, T-fimbrin; domain 1 ...Autophagy protein 6/Beclin 1 / Beclin-1, BH3 domain / Beclin-1 BH3 domain, Bcl-2-interacting / Atg6/Beclin / Atg6/Beclin C-terminal domain superfamily / Atg6, BARA domain / Atg6/beclin, coiled-coil domain / Apg6 BARA domain / Apg6 coiled-coil region / Actin-binding Protein, T-fimbrin; domain 1 / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 1.547 Å
AuthorsHuang, W.J. / Choi, W.Y. / Wang, J.W. / Shi, Y.G.
CitationJournal: Cell Res. / Year: 2012
Title: Crystal structure and biochemical analyses reveal Beclin 1 as a novel membrane binding protein
Authors: Huang, W. / Choi, W. / Hu, W. / Mi, N. / Guo, Q. / Ma, M. / Liu, M. / Tian, Y. / Lu, P. / Wang, F.L. / Deng, H. / Liu, L. / Gao, N. / Yu, L. / Shi, Y.
History
DepositionJan 19, 2012Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Feb 22, 2012Provider: repository / Type: Initial release
Revision 1.1Mar 20, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Beclin-1


Theoretical massNumber of molelcules
Total (without water)24,4601
Polymers24,4601
Non-polymers00
Water2,072115
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)80.746, 33.563, 74.765
Angle α, β, γ (deg.)90.00, 113.49, 90.00
Int Tables number5
Space group name H-MC121

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Components

#1: Protein Beclin-1 / Coiled-coil myosin-like BCL2-interacting protein / Protein GT197


Mass: 24459.807 Da / Num. of mol.: 1 / Fragment: UNP residues 241-450
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: BECN1, GT197 / Production host: Escherichia coli (E. coli) / References: UniProt: Q14457
#2: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 115 / 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: 1.9 Å3/Da / Density % sol: 35.24 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop / pH: 8.5
Details: 30% PEG 3350, 0.3M NaCl, 0.1M Tris pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SPring-8 / Beamline: BL41XU / Wavelength: 1 Å
DetectorType: RAYONIX MX-225 / Detector: CCD / Date: Dec 2, 2009
RadiationMonochromator: Si 111 CHANNEL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.547→50 Å / Num. obs: 26572 / % possible obs: 97.8 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2
Reflection shellResolution: 1.55→1.61 Å / % possible all: 93.3

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Processing

Software
NameVersionClassification
CBASSdata collection
PHASERphasing
PHENIX(phenix.refine: dev_596)refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: SAD / Resolution: 1.547→32.408 Å / FOM work R set: 0.7867 / SU ML: 0.13 / σ(F): 0 / Phase error: 26.89 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2034 1243 5.03 %RANDOM
Rwork0.1755 ---
all0.177 25256 --
obs0.177 24700 90.74 %-
Solvent computationShrinkage radii: 1.01 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 43.947 Å2 / ksol: 0.436 e/Å3
Displacement parametersBiso mean: 40.9722 Å2
Baniso -1Baniso -2Baniso -3
1-19.2043 Å20 Å2-6.5855 Å2
2---9.6744 Å20 Å2
3----9.5299 Å2
Refinement stepCycle: LAST / Resolution: 1.547→32.408 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1590 0 0 115 1705
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0121625
X-RAY DIFFRACTIONf_angle_d1.2742190
X-RAY DIFFRACTIONf_dihedral_angle_d16.034582
X-RAY DIFFRACTIONf_chiral_restr0.083225
X-RAY DIFFRACTIONf_plane_restr0.007277
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 9

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
1.5466-1.60850.32691240.2951205572
1.6085-1.68170.28971500.252235884
1.6817-1.77040.23241120.2132250588
1.7704-1.88130.25791200.1894262992
1.8813-2.02650.20781430.1788272396
2.0265-2.23040.18161480.1614279797
2.2304-2.5530.20161470.1514282598
2.553-3.21610.2141520.1655284098
3.2161-32.41510.17671470.17272592
Refinement TLS params.Method: refined / Origin x: 28.8198 Å / Origin y: -3.9292 Å / Origin z: 17.324 Å
111213212223313233
T0.2124 Å20.0417 Å20.0034 Å2-0.2068 Å20.0037 Å2--0.1896 Å2
L0.8275 °20.2464 °20.0823 °2-1.8621 °20.056 °2--1.5292 °2
S-0.0182 Å °0.022 Å °-0.0268 Å °-0.0437 Å °-0.0418 Å °-0.0853 Å °0.0665 Å °0.1095 Å °0.0077 Å °
Refinement TLS groupSelection details: chain A

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