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- PDB-4ze1: Saccharomyces cerevisiae CYP51 Y140F mutant complexed with posaco... -

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Basic information

Entry
Database: PDB / ID: 4ze1
TitleSaccharomyces cerevisiae CYP51 Y140F mutant complexed with posaconazole in the active site
ComponentsLanosterol 14-alpha demethylase
Keywordsoxidoreductase/oxidoreductase inhibitor / CYP51 / oxidoreductase-oxidoreductase inhibitor complex / resistance mutation
Function / homology
Function and homology information


sterol 14alpha-demethylase / oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen / methyltransferase activity / monooxygenase activity / methylation / iron ion binding / heme binding / membrane
Similarity search - Function
: / Cytochrome P450, E-class, group IV / Cytochrome p450 / Cytochrome P450 / Cytochrome P450, conserved site / Cytochrome P450 cysteine heme-iron ligand signature. / Cytochrome P450 / Cytochrome P450 superfamily / Cytochrome P450 / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
PROTOPORPHYRIN IX CONTAINING FE / POSACONAZOLE / sterol 14alpha-demethylase
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.05 Å
AuthorsSagatova, A. / Keniya, M.V. / Wilson, R. / Tyndall, J.D.A. / Monk, B.C.
Funding support New Zealand, 2items
OrganizationGrant numberCountry
Health Research Council (HRC) New Zealand
Marsden Fund New Zealand
Citation
Journal: Sci Rep / Year: 2016
Title: Triazole resistance mediated by mutations of a conserved active site tyrosine in fungal lanosterol 14 alpha-demethylase.
Authors: Sagatova, A.A. / Keniya, M.V. / Wilson, R.K. / Sabherwal, M. / Tyndall, J.D. / Monk, B.C.
#1: Journal: Proc. Natl. Acad. Sci. U.S.A. / Year: 2014
Title: Architecture of a single membrane spanning cytochrome P450 suggests constraints that orient the catalytic domain relative to a bilayer.
Authors: Monk, B.C. / Tomasiak, T.M. / Keniya, M.V. / Huschmann, F.U. / Tyndall, J.D. / O'Connell, J.D. / Cannon, R.D. / McDonald, J.G. / Rodriguez, A. / Finer-Moore, J.S. / Stroud, R.M.
#2: Journal: To Be Published
Title: Structural insights into binding of the antifungal drug fluconazole to Saccharomyces cerevisiae lanosterol 14alpha-demethylase
Authors: Sagatova, A. / Keniya, M.V. / Wilson, R.K. / Monk, B.C. / Tyndall, J.D.
History
DepositionApr 20, 2015Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 30, 2016Provider: repository / Type: Initial release
Revision 1.1Jun 1, 2016Group: Database references
Revision 1.2Dec 21, 2016Group: Non-polymer description / Structure summary
Revision 1.3Aug 9, 2017Group: Data collection / Database references / Category: diffrn_source / pdbx_related_exp_data_set / Item: _diffrn_source.pdbx_synchrotron_site
Revision 1.4Nov 22, 2017Group: Refinement description / Category: software / Item: _software.classification
Revision 1.5Jan 1, 2020Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.6Sep 27, 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
Revision 1.7Mar 13, 2024Group: Source and taxonomy / Category: entity_src_gen

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Lanosterol 14-alpha demethylase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)63,1863
Polymers61,8691
Non-polymers1,3172
Water2,504139
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)78.790, 67.750, 81.060
Angle α, β, γ (deg.)90.00, 99.43, 90.00
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein Lanosterol 14-alpha demethylase


Mass: 61869.215 Da / Num. of mol.: 1 / Mutation: Y140F
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (strain YJM789) (yeast)
Strain: YJM789 / Gene: ERG11, SCY_2394 / Production host: Saccharomyces cerevisiae (brewer's yeast) / Strain (production host): AD2Delta / References: UniProt: A6ZSR0
#2: Chemical ChemComp-HEM / PROTOPORPHYRIN IX CONTAINING FE / HEME


Mass: 616.487 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C34H32FeN4O4
#3: Chemical ChemComp-X2N / POSACONAZOLE


Mass: 700.777 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C37H42F2N8O4
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 139 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 3.42 Å3/Da / Density % sol: 64 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop / Details: 45% PEG 400, 0.1M Glycine / PH range: 9.3-9.55

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Data collection

DiffractionMean temperature: 93 K
Diffraction sourceSource: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX2 / Wavelength: 0.954 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Feb 20, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.954 Å / Relative weight: 1
ReflectionResolution: 2.05→37.45 Å / Num. obs: 52170 / % possible obs: 98.3 % / Redundancy: 5.5 % / Rmerge(I) obs: 0.082 / Net I/σ(I): 12.9
Reflection shellResolution: 2.05→2.11 Å / Redundancy: 5.5 % / % possible all: 98

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Processing

Software
NameVersionClassification
PHENIX1.8.4_1496refinement
Blu-Icedata collection
Aimlessdata scaling
PHENIXphasing
MOSFLMdata reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4LXJ

4lxj


Resolution: 2.05→29.96 Å / SU ML: 0.28 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 29.69 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.243 2636 5.06 %
Rwork0.203 --
obs0.205 52115 98.2 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.05→29.96 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4270 0 94 139 4503
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0084509
X-RAY DIFFRACTIONf_angle_d1.0796126
X-RAY DIFFRACTIONf_dihedral_angle_d14.3071691
X-RAY DIFFRACTIONf_chiral_restr0.044646
X-RAY DIFFRACTIONf_plane_restr0.005807
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.05-2.08730.4221280.37392591X-RAY DIFFRACTION99
2.0873-2.12740.33411440.32872590X-RAY DIFFRACTION98
2.1274-2.17080.35331370.31092576X-RAY DIFFRACTION98
2.1708-2.2180.34381510.29232571X-RAY DIFFRACTION99
2.218-2.26960.30761470.28442542X-RAY DIFFRACTION97
2.2696-2.32630.28921360.26062598X-RAY DIFFRACTION98
2.3263-2.38920.33151320.24142616X-RAY DIFFRACTION99
2.3892-2.45950.25971350.22042623X-RAY DIFFRACTION98
2.4595-2.53880.24591310.20682598X-RAY DIFFRACTION98
2.5388-2.62950.22991240.21422612X-RAY DIFFRACTION98
2.6295-2.73470.26611420.19992588X-RAY DIFFRACTION99
2.7347-2.85910.25871220.20592636X-RAY DIFFRACTION99
2.8591-3.00970.22361550.20062595X-RAY DIFFRACTION99
3.0097-3.19810.23671410.19822618X-RAY DIFFRACTION99
3.1981-3.44470.24021390.19852610X-RAY DIFFRACTION98
3.4447-3.79070.21821390.18542598X-RAY DIFFRACTION98
3.7907-4.33780.22391630.17022640X-RAY DIFFRACTION100
4.3378-5.45980.17861370.15972683X-RAY DIFFRACTION100
5.4598-29.9590.23541330.18192594X-RAY DIFFRACTION94

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