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- PDB-1j5d: SOLUTION STRUCTURE OF OXIDIZED PARAMAGNETIC CU(II) PLASTOCYANIN F... -

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Basic information

Entry
Database: PDB / ID: 1j5d
TitleSOLUTION STRUCTURE OF OXIDIZED PARAMAGNETIC CU(II) PLASTOCYANIN FROM SYNECHOCYSTIS PCC6803-MINIMIZED AVERAGE STRUCTURE
ComponentsPLASTOCYANIN
KeywordsELECTRON TRANSPORT / copper protein beta barrel electron transfer
Function / homology
Function and homology information


plasma membrane-derived thylakoid membrane / electron transfer activity / copper ion binding
Similarity search - Function
Plastocyanin, cyanobacteria / Plastocyanin / Blue (type 1) copper protein, plastocyanin-type / Blue (type 1) copper domain / Copper binding proteins, plastocyanin/azurin family / Blue (type 1) copper protein, binding site / Type-1 copper (blue) proteins signature. / Cupredoxins - blue copper proteins / Cupredoxin / Immunoglobulin-like ...Plastocyanin, cyanobacteria / Plastocyanin / Blue (type 1) copper protein, plastocyanin-type / Blue (type 1) copper domain / Copper binding proteins, plastocyanin/azurin family / Blue (type 1) copper protein, binding site / Type-1 copper (blue) proteins signature. / Cupredoxins - blue copper proteins / Cupredoxin / Immunoglobulin-like / Sandwich / Mainly Beta
Similarity search - Domain/homology
COPPER (II) ION / Plastocyanin
Similarity search - Component
Biological speciesSynechocystis sp. PCC 6803 (bacteria)
MethodSOLUTION NMR / energy minimization
AuthorsBertini, I. / Ciurli, S. / Dikiy, A. / Fernandez, C.O. / Luchinat, C. / Safarov, N. / Shumilin, S. / Vila, A.J.
CitationJournal: J.Am.Chem.Soc. / Year: 2001
Title: The first solution structure of a paramagnetic copper(II) protein: the case of oxidized plastocyanin from the cyanobacterium Synechocystis PCC6803.
Authors: Bertini, I. / Ciurli, S. / Dikiy, A. / Fernandez, C.O. / Luchinat, C. / Safarov, N. / Shumilin, S. / Vila, A.J.
History
DepositionApr 2, 2002Deposition site: RCSB / Processing site: RCSB
SupersessionApr 10, 2002ID: 1I0Y
Revision 1.0Apr 10, 2002Provider: repository / Type: Initial release
Revision 1.1Apr 26, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Oct 27, 2021Group: Data collection / Database references / Derived calculations
Category: database_2 / pdbx_nmr_software ...database_2 / pdbx_nmr_software / pdbx_nmr_spectrometer / pdbx_struct_assembly / pdbx_struct_conn_angle / pdbx_struct_oper_list / struct_conn / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name / _pdbx_nmr_spectrometer.model / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_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.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_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.pdbx_dist_value / _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_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_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.4Dec 27, 2023Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: PLASTOCYANIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)10,3132
Polymers10,2491
Non-polymers641
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)1 / -
Representative

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Components

#1: Protein PLASTOCYANIN /


Mass: 10249.430 Da / Num. of mol.: 1 / Mutation: D98E
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Synechocystis sp. PCC 6803 (bacteria) / Strain: PCC6803 / Plasmid: PET3D / Production host: Escherichia coli (E. coli) / Strain (production host): BLR(DE3) / References: UniProt: P21697
#2: Chemical ChemComp-CU / COPPER (II) ION / Copper


Mass: 63.546 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cu

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D NOESY
121HNHA
131NOE
141proton T1 (HSQC)

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Sample preparation

DetailsContents: 3 mM plastocyanin U-15N 50 mM phosphate buffer / Solvent system: 90% H2O/10% D2O
Sample conditionsIonic strength: 50 mM phosphate / pH: 5.2 / Pressure: ambient / Temperature: 295 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker AVANCEBrukerAVANCE6001
Bruker AVANCEBrukerAVANCE8002

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Processing

NMR software
NameVersionDeveloperClassification
XwinNMR2Brukercollection
XwinNMR2Brukerdata analysis
XEASY1.3.13Xia, Bartelsdata analysis
DYANA1.5Guentertrefinement
Amber5Kollmanrefinement
RefinementMethod: energy minimization / Software ordinal: 1
Details: The protein contains paramagnetic copper(II), whose electronic relaxation times are quite unfavorable for NMR solution studies. The structure has been solved on the basis of 1041 meaningful ...Details: The protein contains paramagnetic copper(II), whose electronic relaxation times are quite unfavorable for NMR solution studies. The structure has been solved on the basis of 1041 meaningful NOESY cross peaks, 18 1D NOEs, 26 T1 values, 96 dihedral angle constraints and 18 H-bonds. The detection of broad hyperfine shifted signals and their full assignment allowed the identification of the copper(II) ligands and the determination of the Cu-S-C-H dihedral angle for the coordinated cysteine. The global root mean square deviation from the mean structure for the solution structure family is 0.72 and 1.16 for backbone and heavy atoms, respectively. The mean structure from the DYANA family was calculated using MOLMOL and subjected to restrained energy minimization (REM) using the SANDER module of the AMBER 5.0 program package. The force field parameters for all residues, excluded those for the copper-coordinated ligands, were the standard AMBER "all-atoms" parameters. The calculations were performed in vacuo with the distance-dependent dielectric constant option. The non-bonded interactions were evaluated with a cut-off of 10 A. The mixed linear-harmonic flat-bottomed potential implemented in SANDER was applied to all structural constraints. This potential involves a null force constant for structural constraints within the allowed limits, a non-zero harmonic force constant in a small interval outside the allowed limits, and a linearly dependent potential beyond that limit. NOE-derived distance constraints were restricted below the upper distance limit (ri), using a force constant of 32 kcal mol-1 A-2 for the interval ri+0.5 A. Distance constraints involving the same H-bonds used for DYANA calculations were included in the REM calculation, restricting the NH...O and N...O distances to the same upper (ri) values used in DYANA, with a force constant of 32 kcal mol-1 A-2 for the range ri + 0.5 A. The Cu-H distances derived from the analysis of the non-selective longitudinal relaxation rates were also restrained to the same upper (ri) limits used in DYANA, with a force constant of 32 kcal mol-1 A-2 for ri + 0.5 A. The Cu-NHis and Cu-SCys distances were constrained at 2.1+/-0.1 A and 2.2+/-0.1 A, respectively, using a linear-harmonic flat-bottomed potential with force constants of 50 kcal mol-1 A-2 in the 0.3-A distance ranges below and above these limits. The Cu-SMet distance was analogously constrained within the 2.75+/-0.05 A range, using a force constant of 40 kcal mol-1 A-2. The Cu-N(His)-Cg, Cu-N(His)-Ce, Cu-S(Cys)-Cb, Cu-S(Met)-Cg, and Cu-S(Met)-Ce angles were restrained around 127+/-0, 127+/-0, 105+/-5, 130+/-10, 110+/-10, respectively, using a linear-harmonic flat-bottomed potential with force constants of 50 kcal mol-1 deg-2 in the 50 ranges below and above the given values. Analogously, the (His)N-Cu-N(His), (His)N-Cu-S(Cys), (His)N-Cu-S(Met), and (Met)S-Cu-S(Cys) angles were restrained in the 110+/-10, 125+/-15, 95+/-15, and 100+/-10 range with a force constant of 20 kcal mol-1 deg-2 in the 50 angle ranges below and above these limits.
NMR ensembleConformers submitted total number: 1

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