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- PDB-1e60: OXIDIZED DMSO REDUCTASE EXPOSED TO HEPES - Structure II BUFFER -

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Basic information

Entry
Database: PDB / ID: 1.0E+60
TitleOXIDIZED DMSO REDUCTASE EXPOSED TO HEPES - Structure II BUFFER
ComponentsDimethyl sulfoxide/trimethylamine N-oxide reductase
KeywordsOXIDOREDUCTASE / REDUCTASE / DMSO / MOLYBDOPTERIN
Function / homology
Function and homology information


trimethylamine-N-oxide reductase activity / respiratory dimethylsulfoxide reductase / trimethylamine-N-oxide reductase / trimethylamine-N-oxide reductase (cytochrome c) activity / molybdopterin cofactor binding / periplasmic space / metal ion binding
Similarity search - Function
Dimethylsulfoxide Reductase; domain 3 / Dimethylsulfoxide Reductase, domain 3 / Molybdopterin guanine dinucleotide-containing S/N-oxide reductase / Molybdopterin oxidoreductase, N-terminal / Trimethylamine-N-oxide reductase-like, molybdopterin-binding domain / Molybdopterin oxidoreductase N-terminal domain / Dimethylsulfoxide Reductase; domain 2 / Dimethylsulfoxide Reductase, domain 2 / Rossmann fold - #740 / Prokaryotic molybdopterin oxidoreductases signature 2. ...Dimethylsulfoxide Reductase; domain 3 / Dimethylsulfoxide Reductase, domain 3 / Molybdopterin guanine dinucleotide-containing S/N-oxide reductase / Molybdopterin oxidoreductase, N-terminal / Trimethylamine-N-oxide reductase-like, molybdopterin-binding domain / Molybdopterin oxidoreductase N-terminal domain / Dimethylsulfoxide Reductase; domain 2 / Dimethylsulfoxide Reductase, domain 2 / Rossmann fold - #740 / Prokaryotic molybdopterin oxidoreductases signature 2. / Prokaryotic molybdopterin oxidoreductases signature 3. / Molybdopterin oxidoreductase, prokaryotic, conserved site / Molybdopterin dinucleotide-binding domain / Molydopterin dinucleotide binding domain / Barwin-like endoglucanases - #20 / Barwin-like endoglucanases / Aspartate decarboxylase-like domain superfamily / Molybdopterin oxidoreductase / Molybdopterin oxidoreductase / Twin arginine translocation (Tat) signal profile. / Twin-arginine translocation pathway, signal sequence / Alpha-Beta Complex / Beta Barrel / Rossmann fold / 3-Layer(aba) Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
MOLYBDENUM (IV)OXIDE / Chem-PGD / Dimethyl sulfoxide/trimethylamine N-oxide reductase
Similarity search - Component
Biological speciesRhodobacter capsulatus (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å
AuthorsBailey, S. / Bennett, B. / Adams, B. / Smith, A.T. / Bray, R.C.
CitationJournal: Biochemistry / Year: 2000
Title: Reversible Dissociation of Thiolate Ligands from Molybdenum in an Enzyme of the Dimethyl Sulfoxide Reductase Family
Authors: Bray, R.C. / Adams, B. / Smith, A.T. / Bennett, B. / Bailey, S.
History
DepositionAug 6, 2000Deposition site: PDBE / Processing site: PDBE
Revision 1.0Aug 25, 2000Provider: repository / Type: Initial release
Revision 1.1Jun 2, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Nov 6, 2019Group: Advisory / Data collection ...Advisory / Data collection / Database references / Derived calculations / Source and taxonomy / Structure summary
Category: entity / entity_name_com ...entity / entity_name_com / entity_src_nat / pdbx_poly_seq_scheme / pdbx_unobs_or_zero_occ_residues / struct_conn / struct_ref / struct_ref_seq / struct_ref_seq_dif
Item: _entity.pdbx_description / _entity.pdbx_ec ..._entity.pdbx_description / _entity.pdbx_ec / _entity_src_nat.pdbx_beg_seq_num / _entity_src_nat.pdbx_end_seq_num / _entity_src_nat.pdbx_organism_scientific / _entity_src_nat.strain / _pdbx_poly_seq_scheme.pdb_seq_num / _pdbx_unobs_or_zero_occ_residues.auth_seq_id / _struct_conn.pdbx_leaving_atom_flag / _struct_ref.db_code / _struct_ref.pdbx_align_begin / _struct_ref.pdbx_seq_one_letter_code / _struct_ref_seq.pdbx_auth_seq_align_beg

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Dimethyl sulfoxide/trimethylamine N-oxide reductase
C: Dimethyl sulfoxide/trimethylamine N-oxide reductase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)182,64612
Polymers179,0522
Non-polymers3,59410
Water23,7441318
1
A: Dimethyl sulfoxide/trimethylamine N-oxide reductase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)91,3236
Polymers89,5261
Non-polymers1,7975
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
2
C: Dimethyl sulfoxide/trimethylamine N-oxide reductase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)91,3236
Polymers89,5261
Non-polymers1,7975
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
Unit cell
Length a, b, c (Å)68.553, 115.920, 229.649
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121
Noncrystallographic symmetry (NCS)NCS oper: (Code: given
Matrix: (0.03048, -0.07809, -0.99648), (0.50523, -0.85901, 0.08277), (-0.86245, -0.50598, 0.01327)
Vector: 45.48826, 87.24242, 33.02237)

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Components

#1: Protein Dimethyl sulfoxide/trimethylamine N-oxide reductase / TMAOR


Mass: 89525.938 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Rhodobacter capsulatus (bacteria) / Cellular location: PERIPLASM
References: UniProt: Q52675, trimethylamine-N-oxide reductase, respiratory dimethylsulfoxide reductase
#2: Chemical
ChemComp-PGD / 2-AMINO-5,6-DIMERCAPTO-7-METHYL-3,7,8A,9-TETRAHYDRO-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-4-ONE GUANOSINE DINUCLEOTIDE


Mass: 738.541 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C20H24N10O13P2S2
#3: Chemical ChemComp-2MO / MOLYBDENUM (IV)OXIDE


Mass: 127.939 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: MoO2
#4: Chemical
ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: SO4
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 1318 / Source method: isolated from a natural source / Formula: H2O
Compound detailsREDUCES VARIOUS N-OXIDE AND SULFOXIDE COMPOUNDS INCLUDING TRIMETHYLAMINE N-OXIDE DURING ANAEROBIC ...REDUCES VARIOUS N-OXIDE AND SULFOXIDE COMPOUNDS INCLUDING TRIMETHYLAMINE N-OXIDE DURING ANAEROBIC GROWTH USING MOLYBDENUM (MOLYBDOPTERIN)AS COFACTOR.

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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: 45 %
Crystal growpH: 7.5
Details: 0.1M HEPES BUFFER, PH 7.5 2M AMMONIUM SULPHATE 3-4% PEG 400
Crystal grow
*PLUS
Temperature: 20-22 ℃ / pH: 7 / Method: vapor diffusion
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-ID
15 mMsodium phosphate1drop
3100 mMNa+ HEPES1reservoir
42 Mammonium sulfate1reservoir
53-4 %PEG4001reservoir
2enzyme1drop

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: BM14 / Wavelength: 0.97
DetectorType: MARRESEARCH / Detector: IMAGE PLATE / Date: Nov 15, 1998
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97 Å / Relative weight: 1
ReflectionResolution: 2→20 Å / Num. obs: 123010 / % possible obs: 98.1 % / Observed criterion σ(I): 0 / Redundancy: 3.8 % / Biso Wilson estimate: 17 Å2 / Rmerge(I) obs: 0.083 / Net I/σ(I): 5.6
Reflection shellMean I/σ(I) obs: 5.1
Reflection
*PLUS
Num. measured all: 465630

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Processing

Software
NameClassification
REFMACrefinement
MOSFLMdata reduction
CCP4data scaling
CCP4phasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: DMSO REDUCTASE FROM RHODOBACTER CAPSULATUS

Resolution: 2→20 Å / SU B: 4.2 / SU ML: 0.12 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.18 / ESU R Free: 0.16
RfactorNum. reflection% reflectionSelection details
Rfree0.241 6176 5 %EVERY 20TH
Rwork0.194 ---
obs-116649 98.1 %-
Refinement stepCycle: LAST / Resolution: 2→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11868 0 214 1318 13400
Refine LS restraints
Refine-IDTypeDev idealDev ideal target
X-RAY DIFFRACTIONp_bond_d0.0130.02
X-RAY DIFFRACTIONp_angle_d0.0320.04
X-RAY DIFFRACTIONp_angle_deg
X-RAY DIFFRACTIONp_planar_d0.0330.05
X-RAY DIFFRACTIONp_hb_or_metal_coord
X-RAY DIFFRACTIONp_mcbond_it
X-RAY DIFFRACTIONp_mcangle_it
X-RAY DIFFRACTIONp_scbond_it
X-RAY DIFFRACTIONp_scangle_it
X-RAY DIFFRACTIONp_plane_restr
X-RAY DIFFRACTIONp_chiral_restr
X-RAY DIFFRACTIONp_singtor_nbd
X-RAY DIFFRACTIONp_multtor_nbd
X-RAY DIFFRACTIONp_xhyhbond_nbd
X-RAY DIFFRACTIONp_xyhbond_nbd
X-RAY DIFFRACTIONp_planar_tor
X-RAY DIFFRACTIONp_staggered_tor
X-RAY DIFFRACTIONp_orthonormal_tor
X-RAY DIFFRACTIONp_transverse_tor
X-RAY DIFFRACTIONp_special_tor
Software
*PLUS
Name: REFMAC / Classification: refinement
Refinement
*PLUS
Lowest resolution: 30 Å / Rfactor obs: 0.194
Solvent computation
*PLUS
Displacement parameters
*PLUS

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