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- PDB-6r42: Structure of R504C mutant of Pseudomonas aeruginosa Penicillin-Bi... -

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Basic information

Database: PDB / ID: 6r42
TitleStructure of R504C mutant of Pseudomonas aeruginosa Penicillin-Binding Protein 3 (PBP3) in complex with piperacillin
ComponentsPeptidoglycan D,D-transpeptidase FtsI
KeywordsHYDROLASE / penicillin-binding protein / peptidoglycan / Transpeptidase
Function / homology
Function and homology information

peptidoglycan glycosyltransferase activity / serine-type D-Ala-D-Ala carboxypeptidase / FtsZ-dependent cytokinesis / division septum assembly / serine-type D-Ala-D-Ala carboxypeptidase activity / penicillin binding / peptidoglycan biosynthetic process / cell wall organization / regulation of cell shape / proteolysis / plasma membrane
Similarity search - Function
Peptidoglycan D,D-transpeptidase FtsI / Penicillin-binding protein, dimerisation domain / Penicillin-binding Protein dimerisation domain / Penicillin-binding protein, dimerisation domain superfamily / Penicillin-binding protein, transpeptidase / Penicillin binding protein transpeptidase domain / Beta-lactamase/transpeptidase-like
Similarity search - Domain/homology
Piperacillin (Open Form) / Peptidoglycan D,D-transpeptidase FtsI
Similarity search - Component
Biological speciesPseudomonas aeruginosa (bacteria)
AuthorsBellini, D. / Dowson, C.G.
Funding support United Kingdom, 1items
OrganizationGrant numberCountry
Medical Research Council (United Kingdom)grant.MR/P007503/1 United Kingdom
CitationJournal: J.Mol.Biol. / Year: 2019
Title: Novel and Improved Crystal Structures of H. influenzae, E. coli and P. aeruginosa Penicillin-Binding Protein 3 (PBP3) and N. gonorrhoeae PBP2: Toward a Better Understanding of beta-Lactam ...Title: Novel and Improved Crystal Structures of H. influenzae, E. coli and P. aeruginosa Penicillin-Binding Protein 3 (PBP3) and N. gonorrhoeae PBP2: Toward a Better Understanding of beta-Lactam Target-Mediated Resistance.
Authors: Bellini, D. / Koekemoer, L. / Newman, H. / Dowson, C.G.
DepositionMar 21, 2019Deposition site: PDBE / Processing site: PDBE
Revision 1.0Feb 19, 2020Provider: repository / Type: Initial release
Revision 1.1Jan 24, 2024Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Deposited unit
A: Peptidoglycan D,D-transpeptidase FtsI
hetero molecules

Theoretical massNumber of molelcules
Total (without water)58,4932

  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area0 Å2
ΔGint0 kcal/mol
Surface area23470 Å2
Unit cell
Length a, b, c (Å)68.440, 82.640, 88.760
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121


#1: Protein Peptidoglycan D,D-transpeptidase FtsI / Penicillin-binding protein 3 / PBP-3

Mass: 57972.992 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (bacteria)
Gene: ftsI, pbpB, PA4418 / Production host: Escherichia coli (E. coli)
References: UniProt: G3XD46, serine-type D-Ala-D-Ala carboxypeptidase
#2: Chemical ChemComp-JPP / Piperacillin (Open Form)

Mass: 519.571 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C23H29N5O7S / Feature type: SUBJECT OF INVESTIGATION
#3: Water ChemComp-HOH / water / Water

Mass: 18.015 Da / Num. of mol.: 118 / Source method: isolated from a natural source / Formula: H2O

Experimental details


ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

Sample preparation

CrystalDensity Matthews: 2.15 Å3/Da / Density % sol: 42.69 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop
Details: 25% (w/v) polyethylene glycol 3 350, 0.1 M Bis-Tris propane pH 7.8 and 1% (w/v) protamine sulphate

Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I04 / Wavelength: 0.98 Å
DetectorType: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Sep 4, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.98 Å / Relative weight: 1
ReflectionResolution: 1.72→54.23 Å / Num. obs: 54141 / % possible obs: 100 % / Redundancy: 11.5 % / Net I/σ(I): 13.8
Reflection shellResolution: 1.72→1.75 Å / Num. unique obs: 2641 / CC1/2: 0.5


DIALSdata reduction
Aimlessdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3OC2
Resolution: 1.72→54.2 Å / Cor.coef. Fo:Fc: 0.958 / Cor.coef. Fo:Fc free: 0.934 / SU B: 4.176 / SU ML: 0.123 / Cross valid method: THROUGHOUT / ESU R: 0.125 / ESU R Free: 0.124 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.25055 2761 5.1 %RANDOM
Rwork0.20846 ---
obs0.21061 51309 99.88 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å
Displacement parametersBiso mean: 33.939 Å2
Baniso -1Baniso -2Baniso -3
1-2.95 Å2-0 Å20 Å2
2---0.93 Å2-0 Å2
3----2.02 Å2
Refinement stepCycle: 1 / Resolution: 1.72→54.2 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3975 0 0 118 4093
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.020.0194051
X-RAY DIFFRACTIONr_bond_other_d0.0020.023950
X-RAY DIFFRACTIONr_angle_refined_deg2.0021.9775501
X-RAY DIFFRACTIONr_angle_other_deg1.13939058
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.0875516
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.08623.294170
X-RAY DIFFRACTIONr_dihedral_angle_3_deg15.60815663
X-RAY DIFFRACTIONr_dihedral_angle_4_deg17.1311536
X-RAY DIFFRACTIONr_chiral_restr0.1620.2618
X-RAY DIFFRACTIONr_gen_planes_refined0.0110.0214622
X-RAY DIFFRACTIONr_gen_planes_other0.0020.02912
X-RAY DIFFRACTIONr_nbd_refined
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_it2.9083.0962067
X-RAY DIFFRACTIONr_mcbond_other2.9013.0932066
X-RAY DIFFRACTIONr_mcangle_it4.184.6282582
X-RAY DIFFRACTIONr_mcangle_other4.184.6322583
X-RAY DIFFRACTIONr_scbond_it3.83.5931984
X-RAY DIFFRACTIONr_scbond_other3.7993.5961985
X-RAY DIFFRACTIONr_scangle_other5.5945.2072920
X-RAY DIFFRACTIONr_long_range_B_refined7.33936.9384388
X-RAY DIFFRACTIONr_long_range_B_other7.33636.9534381
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 1.72→1.765 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.397 208 -
Rwork0.365 3711 -
obs--99.95 %

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