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- PDB-2y3s: Structure of the tirandamycine-bound FAD-dependent tirandamycin o... -

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Basic information

Entry
Database: PDB / ID: 2y3s
TitleStructure of the tirandamycine-bound FAD-dependent tirandamycin oxidase TamL in C2 space group
ComponentsTAML
KeywordsOXIDOREDUCTASE
Function / homology
Function and homology information


FAD binding / oxidoreductase activity / metal ion binding
Similarity search - Function
: / Vanillyl-alcohol Oxidase; Chain A, domain 3 - #20 / Berberine/berberine-like / Berberine and berberine like / Oxygen oxidoreductase covalent FAD-binding site / Oxygen oxidoreductases covalent FAD-binding site. / Vanillyl-alcohol Oxidase; Chain A, domain 3 / Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 3 - #10 / Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 3 / FAD linked oxidase, N-terminal ...: / Vanillyl-alcohol Oxidase; Chain A, domain 3 - #20 / Berberine/berberine-like / Berberine and berberine like / Oxygen oxidoreductase covalent FAD-binding site / Oxygen oxidoreductases covalent FAD-binding site. / Vanillyl-alcohol Oxidase; Chain A, domain 3 / Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 3 - #10 / Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 3 / FAD linked oxidase, N-terminal / FAD binding domain / FAD-binding domain, PCMH-type / PCMH-type FAD-binding domain profile. / FAD-binding, type PCMH, subdomain 2 / FAD-binding, type PCMH-like superfamily / 2-Layer Sandwich / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
FLAVIN-ADENINE DINUCLEOTIDE / TIRANDAMYCIN E / TamL
Similarity search - Component
Biological speciesSTREPTOMYCES SP. 307-9 (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.67 Å
AuthorsCarlson, J.C. / Li, S. / Gunatilleke, S.S. / Anzai, Y. / Burr, D.A. / Podust, L.M. / Sherman, D.H.
CitationJournal: Nat.Chem / Year: 2011
Title: Tirandamycin Biosynthesis is Mediated by Co-Dependent Oxidative Enzymes
Authors: Carlson, J.C. / Li, S. / Gunatilleke, S.S. / Anzai, Y. / Burr, D.A. / Podust, L.M. / Sherman, D.H.
History
DepositionDec 23, 2010Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jun 29, 2011Provider: repository / Type: Initial release
Revision 1.1Aug 3, 2011Group: Database references / Non-polymer description / Version format compliance
Revision 1.2May 8, 2019Group: Data collection / Derived calculations ...Data collection / Derived calculations / Experimental preparation / Other
Category: exptl_crystal_grow / pdbx_database_proc ...exptl_crystal_grow / pdbx_database_proc / pdbx_database_status / pdbx_struct_special_symmetry / struct_biol / struct_conn
Item: _exptl_crystal_grow.temp / _pdbx_database_status.recvd_author_approval / _struct_conn.pdbx_leaving_atom_flag
Revision 1.3Dec 20, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_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_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.4Oct 9, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature / Item: _pdbx_entry_details.has_protein_modification

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: TAML
B: TAML
hetero molecules


Theoretical massNumber of molelcules
Total (without water)119,44418
Polymers116,3792
Non-polymers3,06416
Water15,997888
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8540 Å2
ΔGint-85.1 kcal/mol
Surface area33810 Å2
MethodPISA
Unit cell
Length a, b, c (Å)162.046, 105.786, 70.971
Angle α, β, γ (deg.)90.00, 110.67, 90.00
Int Tables number5
Space group name H-MC121
Components on special symmetry positions
IDModelComponents
11A-2168-

HOH

21B-2043-

HOH

Noncrystallographic symmetry (NCS)NCS oper: (Code: given
Matrix: (0.7539, -0.02881, 0.6563), (-0.03212, -0.9995, -0.006973), (0.6562, -0.01583, -0.7544)
Vector: -2.781, -26.61, 6.274)

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Components

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Protein , 1 types, 2 molecules AB

#1: Protein TAML


Mass: 58189.711 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Details: COVALENT LINK BETWEEN 8-ALPHA METHYL GROUP OF FAD TO N-1 OF HIS 62. COVALENT LINK BETWEEN C-6 ATOM OF FAD AND CYS 122
Source: (gene. exp.) STREPTOMYCES SP. 307-9 (bacteria) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): CODON PLUS RP / References: UniProt: D3Y1I2

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Non-polymers , 6 types, 904 molecules

#2: Chemical ChemComp-FAD / FLAVIN-ADENINE DINUCLEOTIDE


Mass: 785.550 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C27H33N9O15P2 / Comment: FAD*YM
#3: Chemical ChemComp-TIR / TIRANDAMYCIN E


Mass: 403.469 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C22H29NO6
#4: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg
#5: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C3H8O3
#6: Chemical
ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: Cl
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 888 / Source method: isolated from a natural source / Formula: H2O

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Details

Has protein modificationY
Nonpolymer detailsFLAVIN-ADENINE DINUCLEOTIDE (FAD): COVALENT LINK BETWEEN 8-ALPHA METHYL GROUP OF FAD TO N-1 OF HIS ...FLAVIN-ADENINE DINUCLEOTIDE (FAD): COVALENT LINK BETWEEN 8-ALPHA METHYL GROUP OF FAD TO N-1 OF HIS 62. COVALENT LINK BETWEEN C-6 ATOM OF FAD AND CYS 122. TIRANDAMYCIN E (TIR): TAML SUBSTRATE. GLYCEROL (GOL): COMPONENT OF CRYO-PROTECTANT. MAGNESIUM ION (MG): COORDINATED TO TIRANDAMYCIN AND FOUR WATER MOLECULES.
Sequence detailsHIS8-TAG AND TEV PROTEASE SITE ARE ENGINEERED AT THE N- TERMINUS.

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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: 2.59 Å3/Da / Density % sol: 52.48 % / Description: NONE
Crystal growTemperature: 296 K / pH: 7.5 / Details: 9% PEG 4000, 0.2M MGSO4, 23 DEGREES C., pH 7.5

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Data collection

DiffractionMean temperature: 110 K
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 8.3.1 / Wavelength: 1.11587
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Dec 4, 2010 / Details: MIRRORS
RadiationMonochromator: SI (111) DOUBLE CRYSTAL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.11587 Å / Relative weight: 1
ReflectionResolution: 1.67→86.76 Å / Num. obs: 120184 / % possible obs: 92.9 % / Observed criterion σ(I): 1.5 / Redundancy: 3.8 % / Rmerge(I) obs: 0.11 / Net I/σ(I): 6.2
Reflection shellResolution: 1.67→1.76 Å / Redundancy: 2.5 % / Rmerge(I) obs: 0.51 / Mean I/σ(I) obs: 1.4 / % possible all: 64.2

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Processing

Software
NameVersionClassification
REFMAC5.5.0109refinement
MOSFLMdata reduction
SCALAdata scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2Y08

2y08


Resolution: 1.67→86.76 Å / Cor.coef. Fo:Fc: 0.959 / Cor.coef. Fo:Fc free: 0.93 / SU B: 4.786 / SU ML: 0.071 / Cross valid method: THROUGHOUT / ESU R: 0.142 / ESU R Free: 0.107 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES REFINED INDIVIDUALLY
RfactorNum. reflection% reflectionSelection details
Rfree0.22039 6026 5 %RANDOM
Rwork0.1606 ---
obs0.16358 114137 92.8 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 18.15 Å2
Baniso -1Baniso -2Baniso -3
1-1.12 Å20 Å20.86 Å2
2--1.59 Å20 Å2
3----2.1 Å2
Refinement stepCycle: LAST / Resolution: 1.67→86.76 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms7599 0 201 888 8688
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0260.0218199
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg2.0961.97111269
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.36951047
X-RAY DIFFRACTIONr_dihedral_angle_2_deg26.9722.459370
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.768151163
X-RAY DIFFRACTIONr_dihedral_angle_4_deg19.0611582
X-RAY DIFFRACTIONr_chiral_restr0.1530.21208
X-RAY DIFFRACTIONr_gen_planes_refined0.0130.0216478
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it2.1011.55028
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it3.07628096
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it4.88133171
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it6.7824.53152
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr2.60638199
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 1.67→1.713 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.408 246 -
Rwork0.321 5201 -
obs--57.19 %

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