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- PDB-6uxq: Crystal structure of BAK core domain BH3-groove-dimer in complex ... -

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Basic information

Entry
Database: PDB / ID: 6uxq
TitleCrystal structure of BAK core domain BH3-groove-dimer in complex with POPC and C8E4
ComponentsBcl-2 homologous antagonist/killer
KeywordsAPOPTOSIS / Pore-forming Protein
Function / homology
Function and homology information


Activation and oligomerization of BAK protein / response to mycotoxin / B cell negative selection / BAK complex / BH domain binding / apoptotic process involved in blood vessel morphogenesis / negative regulation of endoplasmic reticulum calcium ion concentration / response to fungus / limb morphogenesis / Release of apoptotic factors from the mitochondria ...Activation and oligomerization of BAK protein / response to mycotoxin / B cell negative selection / BAK complex / BH domain binding / apoptotic process involved in blood vessel morphogenesis / negative regulation of endoplasmic reticulum calcium ion concentration / response to fungus / limb morphogenesis / Release of apoptotic factors from the mitochondria / post-embryonic camera-type eye morphogenesis / endocrine pancreas development / establishment or maintenance of transmembrane electrochemical gradient / positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway / B cell apoptotic process / negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway / activation of cysteine-type endopeptidase activity / endoplasmic reticulum calcium ion homeostasis / positive regulation of endoplasmic reticulum unfolded protein response / regulation of mitochondrial membrane permeability / calcium ion transport into cytosol / response to UV-C / mitochondrial fusion / fibroblast apoptotic process / Bcl-2 family protein complex / myeloid cell homeostasis / positive regulation of calcium ion transport into cytosol / porin activity / thymocyte apoptotic process / pore complex / negative regulation of release of cytochrome c from mitochondria / positive regulation of proteolysis / positive regulation of IRE1-mediated unfolded protein response / positive regulation of release of cytochrome c from mitochondria / vagina development / B cell homeostasis / intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress / cellular response to unfolded protein / blood vessel remodeling / animal organ regeneration / Pyroptosis / negative regulation of peptidyl-serine phosphorylation / extrinsic apoptotic signaling pathway in absence of ligand / heat shock protein binding / intrinsic apoptotic signaling pathway / release of cytochrome c from mitochondria / regulation of mitochondrial membrane potential / epithelial cell proliferation / establishment of localization in cell / response to gamma radiation / apoptotic signaling pathway / positive regulation of protein-containing complex assembly / response to hydrogen peroxide / response to organic cyclic compound / cellular response to mechanical stimulus / cellular response to UV / intrinsic apoptotic signaling pathway in response to DNA damage / protein-folding chaperone binding / response to ethanol / mitochondrial outer membrane / transmembrane transporter binding / regulation of cell cycle / response to xenobiotic stimulus / positive regulation of apoptotic process / protein heterodimerization activity / negative regulation of cell population proliferation / negative regulation of gene expression / apoptotic process / protein-containing complex binding / endoplasmic reticulum / protein homodimerization activity / mitochondrion / identical protein binding / metal ion binding / cytosol
Similarity search - Function
Apoptosis regulator, Bcl-2, BH3 motif, conserved site / Apoptosis regulator, Bcl-2 family BH3 motif signature. / Apoptosis regulator, Bcl-2, BH1 motif, conserved site / Apoptosis regulator, Bcl-2 family BH1 motif signature. / Apoptosis regulator, Bcl-2, BH2 motif, conserved site / Apoptosis regulator, Bcl-2 family BH2 motif signature. / BCL (B-Cell lymphoma); contains BH1, BH2 regions / Bcl-2 family / Bcl-2, Bcl-2 homology region 1-3 / Bcl2-like ...Apoptosis regulator, Bcl-2, BH3 motif, conserved site / Apoptosis regulator, Bcl-2 family BH3 motif signature. / Apoptosis regulator, Bcl-2, BH1 motif, conserved site / Apoptosis regulator, Bcl-2 family BH1 motif signature. / Apoptosis regulator, Bcl-2, BH2 motif, conserved site / Apoptosis regulator, Bcl-2 family BH2 motif signature. / BCL (B-Cell lymphoma); contains BH1, BH2 regions / Bcl-2 family / Bcl-2, Bcl-2 homology region 1-3 / Bcl2-like / Apoptosis regulator proteins, Bcl-2 family / BCL2-like apoptosis inhibitors family profile. / Bcl-2-like superfamily
Similarity search - Domain/homology
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine / Bcl-2 homologous antagonist/killer
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 1.696 Å
AuthorsCowan, A.D. / Colman, P.M. / Czabotar, P.E.
Funding support Australia, 3items
OrganizationGrant numberCountry
National Health and Medical Research Council (NHMRC, Australia)1079706 Australia
National Health and Medical Research Council (NHMRC, Australia)1059290 Australia
National Health and Medical Research Council (NHMRC, Australia)1113133 Australia
CitationJournal: Nat.Struct.Mol.Biol. / Year: 2020
Title: BAK core dimers bind lipids and can be bridged by them.
Authors: Cowan, A.D. / Smith, N.A. / Sandow, J.J. / Kapp, E.A. / Rustam, Y.H. / Murphy, J.M. / Brouwer, J.M. / Bernardini, J.P. / Roy, M.J. / Wardak, A.Z. / Tan, I.K. / Webb, A.I. / Gulbis, J.M. / ...Authors: Cowan, A.D. / Smith, N.A. / Sandow, J.J. / Kapp, E.A. / Rustam, Y.H. / Murphy, J.M. / Brouwer, J.M. / Bernardini, J.P. / Roy, M.J. / Wardak, A.Z. / Tan, I.K. / Webb, A.I. / Gulbis, J.M. / Smith, B.J. / Reid, G.E. / Dewson, G. / Colman, P.M. / Czabotar, P.E.
History
DepositionNov 7, 2019Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 2, 2020Provider: repository / Type: Initial release
Revision 1.1Sep 30, 2020Group: 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.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Nov 18, 2020Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation_author.identifier_ORCID
Revision 1.3Oct 11, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Bcl-2 homologous antagonist/killer
B: Bcl-2 homologous antagonist/killer
C: Bcl-2 homologous antagonist/killer
D: Bcl-2 homologous antagonist/killer
hetero molecules


Theoretical massNumber of molelcules
Total (without water)41,78520
Polymers38,0034
Non-polymers3,78216
Water2,630146
1
A: Bcl-2 homologous antagonist/killer
B: Bcl-2 homologous antagonist/killer
hetero molecules


Theoretical massNumber of molelcules
Total (without water)22,07415
Polymers19,0012
Non-polymers3,07313
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5250 Å2
ΔGint-61 kcal/mol
Surface area9350 Å2
MethodPISA
2
C: Bcl-2 homologous antagonist/killer
D: Bcl-2 homologous antagonist/killer
hetero molecules


Theoretical massNumber of molelcules
Total (without water)19,7105
Polymers19,0012
Non-polymers7093
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5090 Å2
ΔGint-49 kcal/mol
Surface area11450 Å2
MethodPISA
Unit cell
Length a, b, c (Å)84.318, 150.086, 51.749
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number20
Space group name H-MC2221
Components on special symmetry positions
IDModelComponents
11C-321-

HOH

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Components

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Protein , 1 types, 4 molecules ABCD

#1: Protein
Bcl-2 homologous antagonist/killer / Apoptosis regulator BAK / Bcl-2-like protein 7 / Bcl2-L-7


Mass: 9500.688 Da / Num. of mol.: 4 / Fragment: Core/dimerisation domain, residues 68-148
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: BAK1, BAK, BCL2L7, CDN1 / Plasmid: pGEX-6P-3 / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: Q16611

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Non-polymers , 5 types, 162 molecules

#2: Chemical
ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: SO4
#3: Chemical
ChemComp-C8E / (HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE


Mass: 306.438 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C16H34O5 / Comment: C8E, detergent*YM
#4: Chemical ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL / Ethylene glycol


Mass: 62.068 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C2H6O2
#5: Chemical ChemComp-LBN / 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine / (2R)-2-[(9Z)-9-Octadecenoyloxy]-3-(palmitoyloxy)propyl 2-(trimethylammonio)ethyl phosphate / POPC


Mass: 760.076 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C42H82NO8P / Feature type: SUBJECT OF INVESTIGATION / Comment: phospholipid*YM
#6: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 146 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestY

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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: 2.15 Å3/Da / Density % sol: 42.9 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 5.5
Details: ammonium sulphate, trisodium citrate, tetraethylene glycol monooctyl ether, 1-palmitoyl-2-oleoyl-glycero-3-phosphocholine

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX2 / Wavelength: 0.9537 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Jul 27, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9537 Å / Relative weight: 1
ReflectionResolution: 1.696→43.025 Å / Num. obs: 36562 / % possible obs: 99.2 % / Redundancy: 7.195 % / Biso Wilson estimate: 32.271 Å2 / CC1/2: 0.998 / Rmerge(I) obs: 0.104 / Rrim(I) all: 0.112 / Χ2: 0.97 / Net I/σ(I): 11.7
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. measured obsNum. possibleNum. unique obsCC1/2Rrim(I) all% possible all
1.7-1.87.1231.5961.4740187588456420.6591.7295.9
1.8-1.927.3220.9532.5740401552055180.8511.024100
1.92-2.087.3440.4764.9537805514851480.960.512100
2.08-2.277.3390.2598.2234998477347690.9840.27999.9
2.27-2.547.3130.15912.2331561431843160.9930.172100
2.54-2.937.2440.10616.9427730383238280.9960.11599.9
2.93-3.597.0310.06625.2123007327532720.9970.07199.9
3.59-5.066.7560.04734.2117336257225660.9980.05199.8
5.06-43.0256.6710.03935.1510027151715030.9990.04299.1

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Phasing

PhasingMethod: molecular replacement
Phasing MR
Highest resolutionLowest resolution
Rotation6.23 Å43.03 Å
Translation6.23 Å43.03 Å

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Processing

Software
NameVersionClassification
PHENIX1.15-3459refinement
XDSdata reduction
XDSdata scaling
PHASER2.6.0phasing
PDB_EXTRACT3.24data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 6UXO

6uxo


Resolution: 1.696→43.025 Å / SU ML: 0.24 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 25.56
RfactorNum. reflection% reflection
Rfree0.214 1992 5.45 %
Rwork0.1791 --
obs0.1811 36543 99.2 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 125.76 Å2 / Biso mean: 34.7259 Å2 / Biso min: 16.73 Å2
Refinement stepCycle: final / Resolution: 1.696→43.025 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2587 0 189 146 2922
Biso mean--57.88 40.87 -
Num. residues----325
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
1.6962-1.73860.43751240.4126221191
1.7386-1.78560.36391470.32362458100
1.7856-1.83820.31741370.27912471100
1.8382-1.89750.2811500.23572429100
1.8975-1.96530.28831370.22352469100
1.9653-2.0440.19981390.1812461100
2.044-2.1370.22621410.16612465100
2.137-2.24970.22521450.15752471100
2.2497-2.39060.18721360.15452482100
2.3906-2.57520.21521460.16582480100
2.5752-2.83430.22851470.16622482100
2.8343-3.24430.24381440.17562506100
3.2443-4.0870.17551450.15222529100
4.087-43.0250.17641540.17532637100
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
10.48320.2213-0.17151.03470.8874.0677-0.02250.03110.0399-0.09780.00340.0055-0.15160.10060.02450.2350.009-0.00290.19880.01570.177825.524237.142112.5719
29.621-3.3548-3.27976.87761.10875.03710.0284-0.5690.27920.76810.0034-0.5682-0.25280.59010.08940.2922-0.0993-0.03910.3580.03250.277539.369139.990835.4988
32.58751.94991.28994.71231.79144.54840.1714-0.299-0.15630.2857-0.2087-0.25170.2111-0.0252-0.00940.23460.02470.0190.27940.03840.237333.989826.028629.9376
42.65031.38890.70092.75130.49693.262-0.13420.07180.11140.08340.1095-0.0606-0.28590.41290.11140.1984-0.0465-0.00610.24520.02870.175934.420837.658124.2218
51.0810.20130.33561.65661.38834.82630.0678-0.0323-0.03090.0749-0.02290.05490.2432-0.0465-0.04250.2636-0.01240.01990.15390.01260.228623.185726.903518.2896
62.26370.34030.04393.21280.33913.2781-0.07360.1907-0.1829-0.2755-0.021-0.23410.20360.18530.09820.23620.00780.03070.25380.00060.194632.553327.13274.3801
73.9457-3.9849-2.97186.3962.63995.39950.17860.6675-0.2771-0.6922-0.61690.546-0.1938-0.59090.38980.3832-0.0205-0.11410.34250.00080.32749.60647.206812.5412
81.07411.1061-0.1966.05410.39281.1744-0.0202-0.0249-0.219-0.3441-0.0018-0.39030.20390.0640.01640.29490.01740.01780.20720.02910.232422.277-1.886215.4036
94.3925-3.2399-3.62326.63853.52746.3590.12530.13830.0977-0.6340.0352-0.1282-0.1393-0.0372-0.16880.2781-0.0499-0.01730.20350.03270.208118.130913.961614.1408
103.61630.39260.96675.76972.97274.08850.1467-0.1831-0.22540.4559-0.39760.74890.2629-0.7050.17340.2026-0.0210.0430.31920.01460.35664.303612.758930.0033
111.86511.18371.50746.673.23334.2178-0.00470.0061-0.06470.03720.0004-0.074-0.15790.02120.02150.201-0.00710.02830.17410.01870.186914.381616.023327.1266
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 64 through 100 )A64 - 100
2X-RAY DIFFRACTION2chain 'A' and (resid 101 through 106 )A101 - 106
3X-RAY DIFFRACTION3chain 'A' and (resid 107 through 124 )A107 - 124
4X-RAY DIFFRACTION4chain 'A' and (resid 125 through 147 )A125 - 147
5X-RAY DIFFRACTION5chain 'B' and (resid 67 through 100 )B67 - 100
6X-RAY DIFFRACTION6chain 'B' and (resid 101 through 146 )B101 - 146
7X-RAY DIFFRACTION7chain 'C' and (resid 69 through 100 )C69 - 100
8X-RAY DIFFRACTION8chain 'C' and (resid 101 through 148 )C101 - 148
9X-RAY DIFFRACTION9chain 'D' and (resid 68 through 100 )D68 - 100
10X-RAY DIFFRACTION10chain 'D' and (resid 101 through 124 )D101 - 124
11X-RAY DIFFRACTION11chain 'D' and (resid 125 through 148 )D125 - 148

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