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- PDB-1zht: Structure of yeast oxysterol binding protein Osh4 in complex with... -

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Basic information

Entry
Database: PDB / ID: 1zht
TitleStructure of yeast oxysterol binding protein Osh4 in complex with 7-hydroxycholesterol
ComponentsKES1 protein
KeywordsLIPID BINDING PROTEIN / Oxysterol sterol binding protein cholesterol
Function / homology
Function and homology information


Acyl chain remodelling of PS / Synthesis of bile acids and bile salts / ER to Golgi ceramide transport / sterol transfer activity / post-Golgi vesicle-mediated transport / sterol transport / sphingolipid metabolic process / maintenance of cell polarity / phosphatidic acid binding / piecemeal microautophagy of the nucleus ...Acyl chain remodelling of PS / Synthesis of bile acids and bile salts / ER to Golgi ceramide transport / sterol transfer activity / post-Golgi vesicle-mediated transport / sterol transport / sphingolipid metabolic process / maintenance of cell polarity / phosphatidic acid binding / piecemeal microautophagy of the nucleus / oxysterol binding / phosphatidylinositol-4-phosphate binding / exocytosis / phosphatidylinositol-4,5-bisphosphate binding / endocytosis / Golgi membrane / lipid binding / membrane / cytoplasm / cytosol
Similarity search - Function
Helix Hairpins - #2720 / Porin - #120 / Alpha-Beta Plaits - #3490 / Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #1430 / Oxysterol-binding protein / Oxysterol-binding protein, conserved site / Oxysterol-binding protein superfamily / Oxysterol-binding protein / Oxysterol-binding protein family signature. / Porin ...Helix Hairpins - #2720 / Porin - #120 / Alpha-Beta Plaits - #3490 / Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #1430 / Oxysterol-binding protein / Oxysterol-binding protein, conserved site / Oxysterol-binding protein superfamily / Oxysterol-binding protein / Oxysterol-binding protein family signature. / Porin / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Helix non-globular / Special / Helix Hairpins / Alpha-Beta Plaits / Beta Barrel / 2-Layer Sandwich / Orthogonal Bundle / Mainly Beta / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
7-HYDROXYCHOLESTEROL / Oxysterol-binding protein homolog 4
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.9 Å
AuthorsIm, Y.J. / Raychaudhuri, S. / Prinz, W.A. / Hurley, J.H.
CitationJournal: Nature / Year: 2005
Title: Structural mechanism for sterol sensing and transport by OSBP-related proteins
Authors: Im, Y.J. / Raychaudhuri, S. / Prinz, W.A. / Hurley, J.H.
History
DepositionApr 26, 2005Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 6, 2005Provider: repository / Type: Initial release
Revision 1.1Apr 30, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Aug 23, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: KES1 protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)50,3012
Polymers49,8981
Non-polymers4031
Water4,684260
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)82.316, 95.080, 65.361
Angle α, β, γ (deg.)90.00, 96.55, 90.00
Int Tables number5
Space group name H-MC121

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Components

#1: Protein KES1 protein / Oxysterol-binding protein homolog 4


Mass: 49898.230 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Gene: OSH4 / Plasmid: modified pGEX4T / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P35844
#2: Chemical ChemComp-HCR / 7-HYDROXYCHOLESTEROL / (3BETA,7BETA)-CHOLEST-5-ENE-3,7-DIOL


Mass: 402.653 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C27H46O2
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 260 / 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: 2.55 Å3/Da / Density % sol: 51.8 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6.5
Details: PEG 20000, MES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K

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Data collection

DiffractionMean temperature: 298 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 22-ID / Wavelength: 1 / Wavelength: 1 Å
DetectorType: MARRESEARCH / Detector: CCD / Date: Dec 10, 2004
RadiationMonochromator: Si 111 CHANNEL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.9→50 Å / Num. all: 39410 / Num. obs: 38269 / % possible obs: 97.1 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 3 / Redundancy: 3.1 % / Biso Wilson estimate: 11.4 Å2 / Rsym value: 0.054 / Net I/σ(I): 16.5
Reflection shellResolution: 1.9→1.97 Å / Mean I/σ(I) obs: 2.9 / Num. unique all: 3362 / Rsym value: 0.222 / % possible all: 85.9

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Processing

Software
NameVersionClassification
CNS1.1refinement
HKL-2000data reduction
SCALEPACKdata scaling
CNSphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entry 1ZHX

1zhx


Resolution: 1.9→43.02 Å / Rfactor Rfree error: 0.004 / Data cutoff high absF: 337440.15 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
RfactorNum. reflection% reflectionSelection details
Rfree0.239 3707 10 %RANDOM
Rwork0.213 ---
all0.22 39410 --
obs0.213 37030 93.9 %-
Solvent computationSolvent model: FLAT MODEL / Bsol: 35.5302 Å2 / ksol: 0.354633 e/Å3
Displacement parametersBiso mean: 22.2 Å2
Baniso -1Baniso -2Baniso -3
1-0.99 Å20 Å21.62 Å2
2--3.98 Å20 Å2
3----4.97 Å2
Refine analyze
FreeObs
Luzzati coordinate error0.26 Å0.23 Å
Luzzati d res low-5 Å
Luzzati sigma a0.21 Å0.16 Å
Refinement stepCycle: LAST / Resolution: 1.9→43.02 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3514 0 29 260 3803
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONc_bond_d0.006
X-RAY DIFFRACTIONc_bond_d_na
X-RAY DIFFRACTIONc_bond_d_prot
X-RAY DIFFRACTIONc_angle_d
X-RAY DIFFRACTIONc_angle_d_na
X-RAY DIFFRACTIONc_angle_d_prot
X-RAY DIFFRACTIONc_angle_deg1.3
X-RAY DIFFRACTIONc_angle_deg_na
X-RAY DIFFRACTIONc_angle_deg_prot
X-RAY DIFFRACTIONc_dihedral_angle_d22.8
X-RAY DIFFRACTIONc_dihedral_angle_d_na
X-RAY DIFFRACTIONc_dihedral_angle_d_prot
X-RAY DIFFRACTIONc_improper_angle_d0.79
X-RAY DIFFRACTIONc_improper_angle_d_na
X-RAY DIFFRACTIONc_improper_angle_d_prot
X-RAY DIFFRACTIONc_mcbond_it
X-RAY DIFFRACTIONc_mcangle_it
X-RAY DIFFRACTIONc_scbond_it
X-RAY DIFFRACTIONc_scangle_it
LS refinement shellResolution: 1.9→2.02 Å / Rfactor Rfree error: 0.013 / Total num. of bins used: 6
RfactorNum. reflection% reflection
Rfree0.286 518 9.7 %
Rwork0.244 4829 -
obs--81.8 %
Xplor file
Refine-IDSerial noParam fileTopol file
X-RAY DIFFRACTION1protein_rep.paramprotein.top
X-RAY DIFFRACTION2ion.paramion.top
X-RAY DIFFRACTION3water.paramwater.top
X-RAY DIFFRACTION47hc.par7hc.top

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