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- PDB-2fta: Structure of Cu(II)azurin with the metal-binding loop sequence "C... -

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Basic information

Entry
Database: PDB / ID: 2fta
TitleStructure of Cu(II)azurin with the metal-binding loop sequence "CTFPGHSALM" replaced with "CTPHPFM"
ComponentsAzurin
KeywordsELECTRON TRANSPORT / Blue copper-binding protein / greek-key beta-barrel
Function / homology
Function and homology information


transition metal ion binding / periplasmic space / electron transfer activity / copper ion binding / zinc ion binding / identical protein binding
Similarity search - Function
Azurin / : / 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 / ETHANOL / DI(HYDROXYETHYL)ETHER / Azurin
Similarity search - Component
Biological speciesPseudomonas aeruginosa (bacteria)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.61 Å
AuthorsBanfield, M.J.
Citation
Journal: Proc.Natl.Acad.Sci.Usa / Year: 2006
Title: Basic requirements for a metal-binding site in a protein: The influence of loop shortening on the cupredoxin azurin.
Authors: Li, C. / Yanagisawa, S. / Martins, B.M. / Messerschmidt, A. / Banfield, M.J. / Dennison, C.
#1: Journal: J.Mol.Biol. / Year: 1991
Title: Crystal structure analysis of oxidized Pseudomonas aeruginosa azurin at pH 5.5 and pH 9.0. A pH-induced conformational transition involves a peptide bond flip
Authors: Nar, H. / Messerschmidt, A. / Huber, R. / van de Kamp, M. / Canters, G.W.
#2: Journal: J.Am.Chem.Soc. / Year: 2004
Title: Loop-contraction mutagenesis of type 1 copper sites
Authors: Yanagisawa, S. / Dennison, C.
#3: Journal: J.Mol.Biol. / Year: 1994
Title: Crystal structure ananlysis and refinement at 2.15 A resolution of amicyanin, a type I blue copper protein, from Thiobacillus versutus
Authors: Romero, A. / Nar, H. / Huber, R. / Messerschmidt, A. / Kalverda, A.P. / Canters, G.W. / Durley, R. / Mathews, F.S.
History
DepositionJan 24, 2006Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 11, 2006Provider: repository / Type: Initial release
Revision 1.1Oct 16, 2007Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Aug 30, 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_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_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_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_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Remark 999SEQUENCE Amino acid sequence CTFPGHSALM, involving residues 132 to 141 in the amino acid database ...SEQUENCE Amino acid sequence CTFPGHSALM, involving residues 132 to 141 in the amino acid database was replaced with the sequence CTPHPM in the deposition

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Azurin
B: Azurin
C: Azurin
D: Azurin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)56,25014
Polymers54,9224
Non-polymers1,32710
Water8,053447
1
A: Azurin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)14,4537
Polymers13,7311
Non-polymers7226
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Azurin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)13,7942
Polymers13,7311
Non-polymers641
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
C: Azurin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)13,7942
Polymers13,7311
Non-polymers641
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
D: Azurin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)14,2093
Polymers13,7311
Non-polymers4782
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)36.840, 97.630, 61.120
Angle α, β, γ (deg.)90.00, 94.31, 90.00
Int Tables number4
Space group name H-MP1211
DetailsThe biological assembly is monomeric (as found in the asymmetric unit)

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Components

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Protein , 1 types, 4 molecules ABCD

#1: Protein
Azurin


Mass: 13730.549 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Pseudomonas aeruginosa (bacteria) / Gene: azu / Plasmid: Trk99a / Production host: Escherichia coli (E. coli) / Strain (production host): JM101 / References: UniProt: P00282

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Non-polymers , 5 types, 457 molecules

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


Mass: 63.546 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Cu
#3: Chemical ChemComp-2PE / NONAETHYLENE GLYCOL


Mass: 414.488 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C18H38O10 / Comment: precipitant*YM
#4: Chemical ChemComp-EOH / ETHANOL


Mass: 46.068 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C2H6O
#5: Chemical ChemComp-PEG / DI(HYDROXYETHYL)ETHER


Mass: 106.120 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C4H10O3
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 447 / Source method: isolated from a natural source / Formula: H2O

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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: 1.99 Å3/Da / Density % sol: 38.34 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7
Details: 0.1M Potassium Thiocyanate, 30% PEG MME 2000, pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: ROTATING ANODE / Type: ENRAF-NONIUS / Wavelength: 1.542 Å
DetectorType: MARRESEARCH / Detector: IMAGE PLATE / Date: Oct 20, 2005
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.542 Å / Relative weight: 1
ReflectionResolution: 1.61→30 Å / Num. all: 55423 / Num. obs: 55423 / % possible obs: 99.4 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.7 % / Biso Wilson estimate: 26.043 Å2 / Rmerge(I) obs: 0.039 / Rsym value: 0.039 / Net I/σ(I): 18.01
Reflection shellResolution: 1.61→1.7 Å / % possible obs: 98.4 % / Rmerge(I) obs: 0.279 / Mean I/σ(I) obs: 4.4 / Num. measured obs: 24724 / Num. unique obs: 8203 / Rsym value: 0.279 / % possible all: 0.987

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Processing

Software
NameVersionClassificationNB
XSCALEdata processing
CNSrefinement
PDB_EXTRACT1.701data extraction
XSCALEdata scaling
AMoREphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 4AZU

4azu


Resolution: 1.61→30 Å / FOM work R set: 0.789 / Isotropic thermal model: isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
RfactorNum. reflectionSelection details
Rfree0.269 1663 RANDOM
Rwork0.233 --
all-55423 -
obs-55423 -
Displacement parametersBiso mean: 25.978 Å2
Refine analyze
FreeObs
Luzzati coordinate error0.29 Å0.24 Å
Luzzati sigma a0.27 Å0.24 Å
Refinement stepCycle: LAST / Resolution: 1.61→30 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3763 0 60 462 4285
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONc_bond_d0.006
X-RAY DIFFRACTIONc_angle_deg1.35
X-RAY DIFFRACTIONc_dihedral_angle_d24.87
X-RAY DIFFRACTIONc_improper_angle_d0.86
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 33

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection obs
1.61-1.630.384460.38114851531
1.63-1.640.334510.3516461697
1.64-1.660.345500.34716191669
1.66-1.680.316510.32116611712
1.68-1.70.325500.29516101660
1.7-1.720.353500.30916141664
1.72-1.740.353520.27816871739
1.74-1.770.349500.29416001650
1.77-1.790.335490.28716041653
1.79-1.820.35510.27316301681
1.82-1.840.311510.25816791730
1.84-1.870.317490.28215731622
1.87-1.90.367510.27316351686
1.9-1.940.272510.26816581709
1.94-1.970.296500.24916261676
1.97-2.010.291510.23316271678
2.01-2.050.278500.24316471697
2.05-2.090.269510.24316191670
2.09-2.140.336500.2516461696
2.14-2.20.26500.24316111661
2.2-2.260.312510.25516351686
2.26-2.320.336510.25416411692
2.32-2.40.286500.26116431693
2.4-2.480.345510.26816521703
2.48-2.580.309500.25915961646
2.58-2.70.292500.24516311681
2.7-2.840.249530.24716921745
2.84-3.020.266490.24716071656
3.02-3.250.242510.21816431694
3.25-3.580.255510.19616411692
3.58-4.10.2520.18316731725
4.1-5.160.181500.1616311681
5.16-500.010.218500.18415981648

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