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- PDB-6yy3: XFEL structure of the Soluble methane monooxygenase hydroxylase a... -

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Basic information

Entry
Database: PDB / ID: 6yy3
TitleXFEL structure of the Soluble methane monooxygenase hydroxylase and regulatory subunit complex, from Methylosinus trichosporium OB3b, t=0 diferrous state prior to oxygen activation
Components
  • (Methane monooxygenase ...) x 2
  • (Methane monooxygenase) x 2
KeywordsOXIDOREDUCTASE / Ferritin superfamily / Soluble methane monooxygenase / Di-iron oxygen activation / Substrate oxidation.
Function / homology
Function and homology information


methane metabolic process / methane monooxygenase (soluble) / methane monooxygenase [NAD(P)H] activity / oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen / one-carbon metabolic process / monooxygenase activity / metal ion binding
Similarity search - Function
: / Monooxygenase component MmoB/DmpM / Monooxygenase component MmoB/DmpM superfamily / MmoB/DmpM family / Methane monooxygenase, gamma chain / Methane monooxygenase, gamma chain, domain 1 / Methane monooxygenase, gamma chain, domain 2 / Methane monooxygenase, gamma chain superfamily / : / : ...: / Monooxygenase component MmoB/DmpM / Monooxygenase component MmoB/DmpM superfamily / MmoB/DmpM family / Methane monooxygenase, gamma chain / Methane monooxygenase, gamma chain, domain 1 / Methane monooxygenase, gamma chain, domain 2 / Methane monooxygenase, gamma chain superfamily / : / : / Methane monooxygenase, hydrolase gamma chain / Methane/phenol monooxygenase, hydroxylase component / Propane/methane/phenol/toluene hydroxylase / Methane/Phenol/Alkene Hydroxylase / Ribonucleotide reductase-like / Ferritin-like superfamily
Similarity search - Domain/homology
: / Methane monooxygenase / Methane monooxygenase / Methane monooxygenase / Methane monooxygenase / Methane monooxygenase component A alpha chain / Methane monooxygenase regulatory protein B
Similarity search - Component
Biological speciesMethylosinus trichosporium OB3b (bacteria)
MethodX-RAY DIFFRACTION / FREE ELECTRON LASER / MOLECULAR REPLACEMENT / Resolution: 2 Å
AuthorsSrinivas, V. / Hogbom, M.
Funding support Sweden, United States, United Kingdom, 15items
OrganizationGrant numberCountry
Swedish Research Council2017-04018 Sweden
European Research Council (ERC)HIGH-GEAR 724394 Sweden
Knut and Alice Wallenberg Foundation2012.0233 Sweden
Knut and Alice Wallenberg Foundation2017.0275 Sweden
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM118030 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM08347 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM133081 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM117126 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM110501 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM126289 United States
Biotechnology and Biological Sciences Research Council (BBSRC)102593 United Kingdom
Wellcome Trust210734/Z/18/Z United Kingdom
Royal SocietyRSWF-R2-182017 United Kingdom
Department of Energy (DOE, United States)DOE BES DE-AC02-05CH11231 United States
Department of Energy (DOE, United States)DOE BES DE-AC02-76SF00515 United States
CitationJournal: J. Am. Chem. Soc. / Year: 2020
Title: High-Resolution XFEL Structure of the Soluble Methane Monooxygenase Hydroxylase Complex with its Regulatory Component at Ambient Temperature in Two Oxidation States.
Authors: Srinivas, V. / Banerjee, R. / Lebrette, H. / Jones, J.C. / Aurelius, O. / Kim, I.S. / Pham, C.C. / Gul, S. / Sutherlin, K.D. / Bhowmick, A. / John, J. / Bozkurt, E. / Fransson, T. / Aller, P. ...Authors: Srinivas, V. / Banerjee, R. / Lebrette, H. / Jones, J.C. / Aurelius, O. / Kim, I.S. / Pham, C.C. / Gul, S. / Sutherlin, K.D. / Bhowmick, A. / John, J. / Bozkurt, E. / Fransson, T. / Aller, P. / Butryn, A. / Bogacz, I. / Simon, P. / Keable, S. / Britz, A. / Tono, K. / Kim, K.S. / Park, S.Y. / Lee, S.J. / Park, J. / Alonso-Mori, R. / Fuller, F.D. / Batyuk, A. / Brewster, A.S. / Bergmann, U. / Sauter, N.K. / Orville, A.M. / Yachandra, V.K. / Yano, J. / Lipscomb, J.D. / Kern, J. / Hogbom, M.
History
DepositionMay 4, 2020Deposition site: PDBE / Processing site: PDBE
Revision 1.0Sep 30, 2020Provider: repository / Type: Initial release
Revision 1.1Jan 24, 2024Group: 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
B: Methane monooxygenase
D: Methane monooxygenase component A alpha chain
F: Methane monooxygenase
G: Methane monooxygenase regulatory protein B
hetero molecules


Theoretical massNumber of molelcules
Total (without water)139,8727
Polymers139,6684
Non-polymers2043
Water8,197455
1
B: Methane monooxygenase
D: Methane monooxygenase component A alpha chain
F: Methane monooxygenase
G: Methane monooxygenase regulatory protein B
hetero molecules

B: Methane monooxygenase
D: Methane monooxygenase component A alpha chain
F: Methane monooxygenase
G: Methane monooxygenase regulatory protein B
hetero molecules


Theoretical massNumber of molelcules
Total (without water)279,74314
Polymers279,3368
Non-polymers4086
Water1448
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation7_645y+1,x-1,-z1
Buried area56030 Å2
ΔGint-276 kcal/mol
Surface area64980 Å2
MethodPISA
Unit cell
Length a, b, c (Å)106.041, 106.041, 301.029
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number92
Space group name H-MP41212
Symmetry operation#1: x,y,z
#2: -y+1/2,x+1/2,z+1/4
#3: y+1/2,-x+1/2,z+3/4
#4: x+1/2,-y+1/2,-z+3/4
#5: -x+1/2,y+1/2,-z+1/4
#6: -x,-y,z+1/2
#7: y,x,-z
#8: -y,-x,-z+1/2

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Components

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Protein , 2 types, 2 molecules BF

#1: Protein Methane monooxygenase


Mass: 45295.340 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Methylosinus trichosporium OB3b (bacteria)
References: UniProt: A0A1A6FJQ4, UniProt: A0A2D2D5X7*PLUS
#3: Protein Methane monooxygenase


Mass: 19444.400 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Methylosinus trichosporium OB3b (bacteria)
References: UniProt: A0A1A6FHH2, UniProt: A0A2D2D0T0*PLUS

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Methane monooxygenase ... , 2 types, 2 molecules DG

#2: Protein Methane monooxygenase component A alpha chain / Methane hydroxylase


Mass: 60031.293 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Methylosinus trichosporium OB3b (bacteria)
References: UniProt: P27353, methane monooxygenase (soluble)
#4: Protein Methane monooxygenase regulatory protein B


Mass: 14896.885 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Methylosinus trichosporium OB3b (bacteria)
Gene: mmoB / Production host: Escherichia coli (E. coli) / References: UniProt: P27356

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Non-polymers , 3 types, 458 molecules

#5: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H8O3
#6: Chemical ChemComp-FE2 / FE (II) ION


Mass: 55.845 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Fe / Feature type: SUBJECT OF INVESTIGATION
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 455 / 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: 3.03 Å3/Da / Density % sol: 59.4 %
Crystal growTemperature: 298 K / Method: vapor diffusion, sitting drop / pH: 7.5
Details: 30 mM Sodium-Iodide, 30 mM Sodium-Bromide, 30 mM Sodium-Fluoride, 20% (v/v) Glycerol, 10% (w/v) PEG 4000, 100 mM Hepes/MOPS pH 7.5 10 mM Iron(III) chloride
Temp details: Room temprature

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Data collection

DiffractionMean temperature: 298 K / Serial crystal experiment: Y
Diffraction sourceSource: FREE ELECTRON LASER / Site: PAL-XFEL / Beamline: NCI / Wavelength: 1.318066 Å
DetectorType: RAYONIX MX225-HS / Detector: CCD / Date: Oct 15, 2019
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.318066 Å / Relative weight: 1
ReflectionResolution: 2→24.66 Å / Num. obs: 116482 / % possible obs: 99.06 % / Redundancy: 81.9 % / Biso Wilson estimate: 41.48 Å2 / CC1/2: 0.933 / Net I/σ(I): 1.994
Reflection shellResolution: 2→2.07 Å / Num. unique obs: 11408 / CC1/2: 0.27 / % possible all: 92.35
Serial crystallography measurementCollection time total: 0.58 hours / Collimation: KB mirrors / Focal spot size: 2.5 µm2 / Pulse duration: 35 fsec. / Pulse energy: 800 µJ / Pulse photon energy: 9.406 keV / XFEL pulse repetition rate: 15 Hz
Serial crystallography sample deliveryDescription: drop on tape combined with acustic droplet ejection
Method: injection
Serial crystallography sample delivery injectionDescription: acustic droplet ejection / Flow rate: 8 µL/min / Injector temperature: 298.15 K / Jet diameter: 260 µm / Power by: focused acoustic pulse
Serial crystallography data reductionFrames total: 31000 / Lattices indexed: 13596 / XFEL run numbers: 169-172

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Processing

Software
NameVersionClassification
PHENIX1.17.1_3660refinement
cctbx.xfeldata reduction
PHASERphasing
cxi.mergedata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 6YD0

6yd0


Resolution: 2→24.66 Å / SU ML: 0.33 / Cross valid method: FREE R-VALUE / Phase error: 25.99 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2337 1977 1.71 %
Rwork0.2036 113534 -
obs0.2041 116482 99.06 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 96.69 Å2 / Biso mean: 45.2607 Å2 / Biso min: 26.42 Å2
Refinement stepCycle: final / Resolution: 2→24.66 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9737 0 8 455 10200
Biso mean--47.23 47.06 -
Num. residues----1209
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 14

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2-2.050.41581200.38627276739690
2.05-2.110.37041380.35837892803098
2.11-2.170.32521410.328580508191100
2.17-2.240.35011400.292880588198100
2.24-2.320.35851420.276480698211100
2.32-2.410.2661420.232381298271100
2.41-2.520.25981410.222280868227100
2.52-2.650.24851420.204881338275100
2.65-2.820.25391420.212381368278100
2.82-3.040.22981440.191581758319100
3.04-3.340.22251430.189482128355100
3.34-3.820.20371440.183982468390100
3.82-4.810.20391450.154483538498100
4.81-24.660.20471530.198587198872100

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