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- PDB-4pi2: Crystal structure of particulate methane monooxygenase from Methy... -

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Basic information

Entry
Database: PDB / ID: 4pi2
TitleCrystal structure of particulate methane monooxygenase from Methylocystis sp. ATCC 49242 (Rockwell) soaked in zinc
Components
  • (Particulate methane monooxygenase subunit ...Methane monooxygenase (particulate)) x 3
  • unknown peptide
KeywordsOXIDOREDUCTASE / Bacterial Proteins / Binding Sites / Copper / Zinc / Methylocystaceae / Oxygenases / Protein Binding
Function / homology
Function and homology information


Particulate methane monooxygenase subunit c2. Chain: C / Helix hairpin bin / particulate methane monooxygenase, chain B / Ammonia/particulate methane monooxygenase, subunit A / Particulate methane monooxygenase, b subunit. Chain: A, domain 3 / Particulate methane monooxygenase, b subunit. Chain: A, domain 1 / Glutathione S-transferase Yfyf (Class Pi); Chain A, domain 2 / Helix Hairpins / Jelly Rolls / Up-down Bundle ...Particulate methane monooxygenase subunit c2. Chain: C / Helix hairpin bin / particulate methane monooxygenase, chain B / Ammonia/particulate methane monooxygenase, subunit A / Particulate methane monooxygenase, b subunit. Chain: A, domain 3 / Particulate methane monooxygenase, b subunit. Chain: A, domain 1 / Glutathione S-transferase Yfyf (Class Pi); Chain A, domain 2 / Helix Hairpins / Jelly Rolls / Up-down Bundle / Immunoglobulin-like / Sandwich / Orthogonal Bundle / Mainly Beta / Mainly Alpha
Similarity search - Domain/homology
CACODYLATE ION / COPPER (II) ION
Similarity search - Component
Biological speciesMethylocystis sp. ATCC 49242 (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / Resolution: 3.33 Å
AuthorsSirajuddin, S. / Rosenzweig, A.C.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM070473 United States
CitationJournal: J.Biol.Chem. / Year: 2014
Title: Effects of zinc on particulate methane monooxygenase activity and structure.
Authors: Sirajuddin, S. / Barupala, D. / Helling, S. / Marcus, K. / Stemmler, T.L. / Rosenzweig, A.C.
History
DepositionMay 7, 2014Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 25, 2014Provider: repository / Type: Initial release
Revision 1.1Jul 9, 2014Group: Database references
Revision 1.2Oct 1, 2014Group: Database references
Revision 1.3Apr 6, 2016Group: Source and taxonomy
Revision 1.4Sep 6, 2017Group: Author supporting evidence / Derived calculations / Category: pdbx_audit_support / pdbx_struct_oper_list
Item: _pdbx_audit_support.funding_organization / _pdbx_struct_oper_list.symmetry_operation
Revision 1.5Dec 25, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.6Dec 27, 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_struct_conn_angle / struct_conn / struct_ncs_dom_lim
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_atom_id / _pdbx_struct_conn_angle.ptnr2_label_comp_id / _pdbx_struct_conn_angle.ptnr2_symmetry / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_conn.ptnr2_symmetry / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
D: unknown peptide
H: unknown peptide
F: Particulate methane monooxygenase subunit A
E: Particulate methane monooxygenase subunit B
N: unknown peptide
A: Particulate methane monooxygenase subunit B
I: Particulate methane monooxygenase subunit B
G: Particulate methane monooxygenase subunit C
J: Particulate methane monooxygenase subunit A
B: Particulate methane monooxygenase subunit A
K: Particulate methane monooxygenase subunit C
C: Particulate methane monooxygenase subunit C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)317,68921
Polymers317,03412
Non-polymers6559
Water0
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area64060 Å2
ΔGint-650 kcal/mol
Surface area86200 Å2
MethodPISA
Unit cell
Length a, b, c (Å)120.857, 185.450, 192.777
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11I
21E
12A
22E
13J
23F
14B
24F
15K
25C
16G
26C

NCS domain segments:

Refine code: 1

Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
111HISHISGLYGLYIG29 - 41729 - 417
211HISHISGLYGLYED29 - 41729 - 417
112HISHISGLYGLYAF29 - 41729 - 417
212HISHISGLYGLYED29 - 41729 - 417
113GLYGLYILEILEJI11 - 25211 - 252
213GLYGLYILEILEFC11 - 25211 - 252
114GLYGLYILEILEBJ11 - 25211 - 252
214GLYGLYILEILEFC11 - 25211 - 252
115GLUGLUGLUGLUKK16 - 21016 - 210
215GLUGLUGLUGLUCL16 - 21016 - 210
125PHEPHEGLUGLUKK224 - 256224 - 256
225PHEPHEGLUGLUCL224 - 256224 - 256
116GLUGLUGLUGLUGH16 - 21016 - 210
216GLUGLUGLUGLUCL16 - 21016 - 210
126PHEPHEGLUGLUGH224 - 256224 - 256
226PHEPHEGLUGLUCL224 - 256224 - 256

NCS ensembles :
ID
1
2
3
4
5
6

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Components

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Protein/peptide , 1 types, 3 molecules DHN

#1: Protein/peptide unknown peptide


Mass: 2145.636 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) Methylocystis sp. ATCC 49242 (bacteria)

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Particulate methane monooxygenase subunit ... , 3 types, 9 molecules FJBEAIGKC

#2: Protein Particulate methane monooxygenase subunit A / Methane monooxygenase (particulate) / pmoA


Mass: 28560.311 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) Methylocystis sp. ATCC 49242 (bacteria) / References: methane monooxygenase (particulate)
#3: Protein Particulate methane monooxygenase subunit B / Methane monooxygenase (particulate) / pmoB


Mass: 45741.105 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) Methylocystis sp. ATCC 49242 (bacteria) / References: methane monooxygenase (particulate)
#4: Protein Particulate methane monooxygenase subunit C / Methane monooxygenase (particulate) / pmoC


Mass: 29231.023 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) Methylocystis sp. ATCC 49242 (bacteria) / References: methane monooxygenase (particulate)

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Non-polymers , 3 types, 9 molecules

#5: Chemical ChemComp-CU / COPPER (II) ION / Copper


Mass: 63.546 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Cu
#6: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: Zn
#7: Chemical ChemComp-CAC / CACODYLATE ION / dimethylarsinate / Cacodylic acid


Mass: 136.989 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C2H6AsO2

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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: 3.55 Å3/Da / Density % sol: 65.31 %
Crystal growTemperature: 295 K / Method: vapor diffusion, sitting drop / pH: 6.5
Details: 10% PEG3000, 0.1 M sodium cacodylate, pH 6.5, 0.2 M magnesium formate dihydrate

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Data collection

DiffractionMean temperature: 110 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 23-ID-D / Wavelength: 1.27816, 1.33765
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Jun 5, 2013
RadiationMonochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
IDWavelength (Å)Relative weight
11.278161
21.337651
ReflectionResolution: 3.33→50 Å / Num. obs: 51611 / % possible obs: 80.4 % / Redundancy: 14.9 % / Net I/σ(I): 23.6

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Processing

Software
NameVersionClassificationNB
REFMAC5.6.0117refinement
PDB_EXTRACT3.14data extraction
RefinementResolution: 3.33→50 Å / Cor.coef. Fo:Fc: 0.857 / Cor.coef. Fo:Fc free: 0.804 / SU B: 28.867 / SU ML: 0.47 / Cross valid method: THROUGHOUT / σ(F): 3 / ESU R Free: 0.673 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT
RfactorNum. reflection% reflectionSelection details
Rfree0.2824 2599 5 %RANDOM
Rwork0.2251 49012 --
obs0.228 51611 80.71 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso max: 207.64 Å2 / Biso mean: 57.249 Å2 / Biso min: 13.9 Å2
Baniso -1Baniso -2Baniso -3
1--0.45 Å20 Å20 Å2
2--1.54 Å20 Å2
3----1.09 Å2
Refinement stepCycle: final / Resolution: 3.33→50 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms20966 0 13 0 20979
Biso mean--88.68 --
Num. residues----2650
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0120.0221618
X-RAY DIFFRACTIONr_angle_refined_deg1.7121.92829518
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.98352635
X-RAY DIFFRACTIONr_dihedral_angle_2_deg37.30622.686927
X-RAY DIFFRACTIONr_dihedral_angle_3_deg21.285153231
X-RAY DIFFRACTIONr_dihedral_angle_4_deg21.13915126
X-RAY DIFFRACTIONr_chiral_restr0.1170.23247
X-RAY DIFFRACTIONr_gen_planes_refined0.0070.02116534
Refine LS restraints NCS

Dom-ID: 1 / Refine-ID: X-RAY DIFFRACTION / Type: TIGHT THERMAL / Weight position: 0.5

Ens-IDAuth asym-IDNumberRms dev position (Å)
1I303013.79
2A303015.37
3J19624.59
4B196212.4
5K18708.22
6G18708.91
LS refinement shellResolution: 3.335→3.421 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.558 9 -
Rwork0.313 277 -
all-286 -
obs--6.19 %

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