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- PDB-2w16: Structures of FpvA bound to heterologous pyoverdines -

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Basic information

Entry
Database: PDB / ID: 2w16
TitleStructures of FpvA bound to heterologous pyoverdines
Components
  • DSN-ARG-DSN-FHO-LYS-FHO-THR-THR
  • FERRIPYOVERDINE RECEPTOR
KeywordsMEMBRANE PROTEIN / FPVA / IRON / MEMBRANE / RECEPTOR / TONB BOX / TRANSPORT / SIDEROPHORE / CELL MEMBRANE / ION TRANSPORT / IRON TRANSPORT / CELL OUTER MEMBRANE / TONB-DEPENDENT TRANSPORTER
Function / homology
Function and homology information


pyoverdine biosynthetic process / siderophore uptake transmembrane transporter activity / cell outer membrane / signaling receptor activity / membrane
Similarity search - Function
Phage tail protein beta-alpha-beta fold - #30 / Phage tail protein beta-alpha-beta fold / Secretin and TonB N terminus short domain / Secretin/TonB, short N-terminal domain / Secretin and TonB N terminus short domain / TonB-dependent receptor, beta-barrel domain / TonB-dependent receptor, plug domain / Maltoporin; Chain A / TonB-dependent siderophore receptor / Ferric Hydroxamate Uptake Protein; Chain A, domain 1 ...Phage tail protein beta-alpha-beta fold - #30 / Phage tail protein beta-alpha-beta fold / Secretin and TonB N terminus short domain / Secretin/TonB, short N-terminal domain / Secretin and TonB N terminus short domain / TonB-dependent receptor, beta-barrel domain / TonB-dependent receptor, plug domain / Maltoporin; Chain A / TonB-dependent siderophore receptor / Ferric Hydroxamate Uptake Protein; Chain A, domain 1 / TonB-dependent receptor, conserved site / TonB-dependent receptor (TBDR) proteins signature 2. / TonB-dependent receptor (TBDR) proteins profile. / Vitamin B12 transporter BtuB-like / TonB-dependent receptor-like, beta-barrel / TonB dependent receptor-like, beta-barrel / TonB-dependent receptor, plug domain superfamily / TonB-dependent receptor, plug domain / TonB-dependent receptor-like, beta-barrel domain superfamily / TonB-dependent Receptor Plug Domain / 3-Layer(bab) Sandwich / Beta Complex / Beta Barrel / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
PYOVERDIN C-E Fe Complex / : / PHOSPHATE ION / Chem-PVE / : / Ferripyoverdine receptor
Similarity search - Component
Biological speciesPSEUDOMONAS AERUGINOSA (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.71 Å
AuthorsGreenwald, J. / Nader, M. / Celia, H. / Gruffaz, C. / Meyer, J.-M. / Schalk, I.J. / Pattus, F.
CitationJournal: Mol.Microbiol. / Year: 2009
Title: Fpva Bound to Non-Cognate Pyoverdines: Molecular Basis of Siderophore Recognition by an Iron Transporter.
Authors: Greenwald, J. / Nader, M. / Celia, H. / Gruffaz, C. / Geoffroy, V. / Meyer, J.M. / Schalk, I.J. / Pattus, F.
History
DepositionOct 14, 2008Deposition site: PDBE / Processing site: PDBE
Revision 1.0May 12, 2009Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Atomic model ...Advisory / Atomic model / Database references / Derived calculations / Non-polymer description / Refinement description / Structure summary / Version format compliance
Revision 1.2Mar 6, 2013Group: Other
Revision 1.3Jun 20, 2018Group: Data collection / Source and taxonomy / Category: diffrn_source / entity_src_gen
Item: _diffrn_source.pdbx_synchrotron_site / _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id
Revision 1.4Jul 10, 2019Group: Data collection / Derived calculations / Category: diffrn_source / struct_conn
Item: _diffrn_source.pdbx_synchrotron_site / _struct_conn.pdbx_leaving_atom_flag
Revision 1.5Jul 24, 2019Group: Data collection / Category: diffrn_source / Item: _diffrn_source.pdbx_synchrotron_site
Revision 1.6Jul 31, 2019Group: Advisory / Data collection / Derived calculations
Category: pdbx_struct_conn_angle / pdbx_validate_close_contact ...pdbx_struct_conn_angle / pdbx_validate_close_contact / struct_conn / struct_conn_type
Item: _struct_conn_type.id
Revision 1.7Dec 13, 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_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.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_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_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Remark 700 SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AE", "BE" IN EACH CHAIN ON SHEET RECORDS ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AE", "BE" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 22-STRANDED BARREL THIS IS REPRESENTED BY A 23-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: FERRIPYOVERDINE RECEPTOR
B: FERRIPYOVERDINE RECEPTOR
C: DSN-ARG-DSN-FHO-LYS-FHO-THR-THR
hetero molecules


Theoretical massNumber of molelcules
Total (without water)176,19217
Polymers174,1093
Non-polymers2,08314
Water0
1
A: FERRIPYOVERDINE RECEPTOR
hetero molecules


Theoretical massNumber of molelcules
Total (without water)87,8279
Polymers86,5561
Non-polymers1,2718
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
2
B: FERRIPYOVERDINE RECEPTOR
C: DSN-ARG-DSN-FHO-LYS-FHO-THR-THR
hetero molecules


Theoretical massNumber of molelcules
Total (without water)88,3658
Polymers87,5532
Non-polymers8126
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1640 Å2
ΔGint-8.5 kcal/mol
Surface area40310 Å2
MethodPQS
Unit cell
Length a, b, c (Å)195.220, 130.082, 141.783
Angle α, β, γ (deg.)90.00, 130.67, 90.00
Int Tables number5
Space group name H-MC121

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Components

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Protein / Protein/peptide , 2 types, 3 molecules ABC

#1: Protein FERRIPYOVERDINE RECEPTOR / FPVA


Mass: 86556.086 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) PSEUDOMONAS AERUGINOSA (bacteria) / Strain: PAO1 / Plasmid: PPVR2 / Production host: PSEUDOMONAS AERUGINOSA (bacteria) / Strain (production host): K691 / References: UniProt: P48632
#2: Protein/peptide DSN-ARG-DSN-FHO-LYS-FHO-THR-THR


Type: PolypeptidePeptide / Class: Metal transport / Mass: 997.062 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: IN IRON-DEFICIENT CONDITIONS, PSEUDOMONAS AERUGINOSA SECRETES A MAJOR FLUORESCENT SIDEROPHORE NAMED PYOVERDIN (PVD), WHICH AFTER CHELATING IRON(III) IS TRANSPORTED BACK INTO THE CELL VIA ITS ...Details: IN IRON-DEFICIENT CONDITIONS, PSEUDOMONAS AERUGINOSA SECRETES A MAJOR FLUORESCENT SIDEROPHORE NAMED PYOVERDIN (PVD), WHICH AFTER CHELATING IRON(III) IS TRANSPORTED BACK INTO THE CELL VIA ITS OUTER MEMBRANE RECEPTOR FPVA. FPVA IS A TONB-DEPENDENT TRANSPORT PROTEIN AND HAS THE ABILITY TO BIND PVD IN ITS APO- OR IRON-LOADED FORM.
Source: (gene. exp.) PSEUDOMONAS AERUGINOSA (bacteria) / Strain: PAO1 / Production host: PSEUDOMONAS AERUGINOSA (bacteria) / Strain (production host): K691 / References: NOR: NOR00190, PYOVERDIN C-E Fe Complex

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Non-polymers , 4 types, 14 molecules

#3: Chemical ChemComp-N8E / 3,6,9,12,15-PENTAOXATRICOSAN-1-OL / N-OCTYLPENTAOXYETHYLENE / PENTAETHYLENE GLYCOL MONOOCTYL ETHER / OCTYLPENTAGLYCOL N-OCTYLPENTAOXYETHYLENE


Mass: 350.491 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C18H38O6 / Comment: C8E5, detergent*YM
#4: Chemical
ChemComp-PO4 / PHOSPHATE ION / Phosphate


Mass: 94.971 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: PO4
#5: Chemical ChemComp-PVE / (1S)-1-CARBOXY-5-[(3-CARBOXYPROPANOYL)AMINO]-8,9-DIHYDROXY-1,2,3,4-TETRAHYDROPYRIMIDO[1,2-A]QUINOLIN-11-IUM


Type: PolypeptidePeptide / Class: Metal transport / Mass: 376.341 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C17H18N3O7
Details: IN IRON-DEFICIENT CONDITIONS, PSEUDOMONAS AERUGINOSA SECRETES A MAJOR FLUORESCENT SIDEROPHORE NAMED PYOVERDIN (PVD), WHICH AFTER CHELATING IRON(III) IS TRANSPORTED BACK INTO THE CELL VIA ITS ...Details: IN IRON-DEFICIENT CONDITIONS, PSEUDOMONAS AERUGINOSA SECRETES A MAJOR FLUORESCENT SIDEROPHORE NAMED PYOVERDIN (PVD), WHICH AFTER CHELATING IRON(III) IS TRANSPORTED BACK INTO THE CELL VIA ITS OUTER MEMBRANE RECEPTOR FPVA. FPVA IS A TONB-DEPENDENT TRANSPORT PROTEIN AND HAS THE ABILITY TO BIND PVD IN ITS APO- OR IRON-LOADED FORM.
References: PYOVERDIN C-E Fe Complex
#6: Chemical ChemComp-FE / FE (III) ION / Iron


Type: PolypeptidePeptide / Class: Metal transport / Mass: 55.845 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Fe
Details: IN IRON-DEFICIENT CONDITIONS, PSEUDOMONAS AERUGINOSA SECRETES A MAJOR FLUORESCENT SIDEROPHORE NAMED PYOVERDIN (PVD), WHICH AFTER CHELATING IRON(III) IS TRANSPORTED BACK INTO THE CELL VIA ITS ...Details: IN IRON-DEFICIENT CONDITIONS, PSEUDOMONAS AERUGINOSA SECRETES A MAJOR FLUORESCENT SIDEROPHORE NAMED PYOVERDIN (PVD), WHICH AFTER CHELATING IRON(III) IS TRANSPORTED BACK INTO THE CELL VIA ITS OUTER MEMBRANE RECEPTOR FPVA. FPVA IS A TONB-DEPENDENT TRANSPORT PROTEIN AND HAS THE ABILITY TO BIND PVD IN ITS APO- OR IRON-LOADED FORM.
References: PYOVERDIN C-E Fe Complex

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Details

Compound detailsPYOVERDINES ARE A GROUP OF STRUCTURALLY RELATED SIDEROPHORES PRODUCED BY FLUORESCENT PSEUDOMONAS ...PYOVERDINES ARE A GROUP OF STRUCTURALLY RELATED SIDEROPHORES PRODUCED BY FLUORESCENT PSEUDOMONAS SPECIES. PYOVERDINE IS NECESSARY FOR INFECTION IN SEVERAL DIFFERENT DISEASE MODELS. THE OCCURRENCE OF PYOVERDINE-DEFECTIVE STRAINS IN CHRONIC INFECTIONS OF PATIENTS WITH CYSTIC FIBROSIS AND THE EXTREMELY HIGH SEQUENCE DIVERSITY OF GENES INVOLVED IN PYOVERDINE SYNTHESIS AND UPTAKE INDICATE THAT PYOVERDINE PRODUCTION IS SUBJECT TO HIGH EVOLUTIONARY PRESSURE. PYOVERDINE-DEPENDENT IRON TRANSPORT IS ALSO CRUCIAL FOR BIOFILM DEVELOPMENT, FURTHER EXPANDING THE IMPORTANCE OF THESE SIDEROPHORES IN PSEUDOMONAS BIOLOGY. GROUP: 1 NAME: FERRIPYOVERDINE FPVA-PVD(G173)-FE COMPLEX CHAIN: C COMPONENT_1: PEPTIDE LIKE SEQUENCE RESIDUES 3 TO 9 COMPONENT_2: PYOVERDINE-CHROMOPHORE RESIDUE PVE 1 COMPONENT_3: FE (III) ION RESIDUE FE 2 DESCRIPTION: IN IRON-DEFICIENT CONDITIONS, PSEUDOMONAS AERUGINOSA SECRETES A MAJOR FLUORESCENT SIDEROPHORE NAMED PYOVERDIN (PVD), WHICH AFTER CHELATING IRON(III) IS TRANSPORTED BACK INTO THE CELL VIA ITS OUTER MEMBRANE RECEPTOR FPVA. FPVA IS A TONB-DEPENDENT TRANSPORT PROTEIN AND HAS THE ABILITY TO BIND PVD IN ITS APO- OR IRON-LOADED FORM.
Nonpolymer details(1S)-5-AMINO-2,3-DIHYDRO-8,9-DIHYDROXY-1H-PYRIMIDO[1, 2A]CHINOLIN-1-CARBOXYLIC ACID (PVE): PVE IS ...(1S)-5-AMINO-2,3-DIHYDRO-8,9-DIHYDROXY-1H-PYRIMIDO[1, 2A]CHINOLIN-1-CARBOXYLIC ACID (PVE): PVE IS LINKED BY A PEPTIDE BOND TO THE SERINE, RESIDUE C 3 OF THE PYOVERDINE PEPTIDE. (O') N5-FORMYL-N5-HYDROXY ORNITHINE (FHO): THERE ARE TWO FHO RESIDUES THAT ARE PART OF THE PYOVERDINE PEPTIDE
Sequence detailsSIGNAL PEPTIDE (RESIDUES 1-43) IS NOT IN THE CRYSTALLIZED PROTEIN.

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 3.96 Å3/Da / Density % sol: 68.67 % / Description: NONE
Crystal growDetails: 1.3M NAH2PO4, 0.1M MES, PH 6.5

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: BW7B / Wavelength: 0.8423
DetectorType: MARRESEARCH / Detector: CCD
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.8423 Å / Relative weight: 1
ReflectionResolution: 2.7→100 Å / Num. obs: 70306 / % possible obs: 95.4 % / Redundancy: 2.3 % / Rmerge(I) obs: 0.08 / Net I/σ(I): 9
Reflection shellResolution: 2.7→2.85 Å / Redundancy: 2.2 % / Rmerge(I) obs: 0.35 / Mean I/σ(I) obs: 2.7 / % possible all: 95.2

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Processing

Software
NameVersionClassification
REFMAC5.4.0054refinement
MOSFLMdata reduction
SCALAdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2O5P

2o5p


Resolution: 2.71→107.83 Å / Cor.coef. Fo:Fc: 0.92 / Cor.coef. Fo:Fc free: 0.893 / SU B: 22.799 / SU ML: 0.215 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.527 / ESU R Free: 0.307 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
RfactorNum. reflection% reflectionSelection details
Rfree0.253 3512 5.1 %RANDOM
Rwork0.217 ---
obs0.219 65796 95.2 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 30.67 Å2
Baniso -1Baniso -2Baniso -3
1-1.35 Å20 Å21.37 Å2
2--0.32 Å20 Å2
3---0.12 Å2
Refinement stepCycle: LAST / Resolution: 2.71→107.83 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms12176 0 125 0 12301
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0170.02212625
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.8311.94617121
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.6644.991534
X-RAY DIFFRACTIONr_dihedral_angle_2_deg38.00724.241639
X-RAY DIFFRACTIONr_dihedral_angle_3_deg19.742151971
X-RAY DIFFRACTIONr_dihedral_angle_4_deg21.4621579
X-RAY DIFFRACTIONr_chiral_restr0.1280.21773
X-RAY DIFFRACTIONr_gen_planes_refined0.0070.0219843
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_it0.6781.57591
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it1.327212203
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it2.29235034
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it3.7814.54918
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.71→2.78 Å / Total num. of bins used: 20 /
RfactorNum. reflection
Rfree0.383 246
Rwork0.334 4792
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
12.987-0.98860.18976.4082-1.63048.27720.09990.0045-0.1917-0.1136-0.22030.41680.8110.24180.1204-0.15790.05540.0663-0.16680.0304-0.0876-10.706-31.81353.541
20.90530.0891-0.21441.1969-0.56811.5430.0036-0.02660.04520.04210.0898-0.0565-0.13580.109-0.0935-0.1798-0.0580.0557-0.2001-0.0822-0.1952-5.059-0.96134.703
39.75961.381-2.8099.7295-0.526310.4271-0.1847-0.49950.19010.09420.22880.4450.00320.0782-0.0441-0.0770.05460.06260.070.10870.0329-29.9134.465-10.031
41.95210.5675-0.42471.1275-0.1991.2423-0.09960.39010.0446-0.19690.02960.0922-0.0469-0.22110.0699-0.1009-0.0611-0.0266-0.0451-0.0182-0.0383-60.333-20.68714.365
55.02-0.1401-5.068.3822-3.14336.87160.29750.03060.1334-0.4760.15980.18070.6302-0.3134-0.4573-0.0101-0.0845-0.03140.1053-0.03130.2005-67.0781-38.554621.2822
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A44 - 129
2X-RAY DIFFRACTION2A130 - 815
3X-RAY DIFFRACTION3B44 - 117
4X-RAY DIFFRACTION4B136 - 815
5X-RAY DIFFRACTION5C3 - 10

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