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- PDB-8bh1: Core divisome complex FtsWIQBL from Pseudomonas aeruginosa -

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Basic information

Entry
Database: PDB / ID: 8bh1
TitleCore divisome complex FtsWIQBL from Pseudomonas aeruginosa
Components
  • Cell division protein FtsB
  • Cell division protein FtsL
  • Cell division protein FtsQ
  • Peptidoglycan D,D-transpeptidase FtsI
  • Probable peptidoglycan glycosyltransferase FtsW
KeywordsMEMBRANE PROTEIN / bacterial cell division / peptidoglycan synthesis / membrane protein complex
Function / homology
Function and homology information


lipid-linked peptidoglycan transporter activity / cell septum assembly / peptidoglycan glycosyltransferase / peptidoglycan glycosyltransferase activity / cell septum / serine-type D-Ala-D-Ala carboxypeptidase / FtsZ-dependent cytokinesis / division septum assembly / serine-type D-Ala-D-Ala carboxypeptidase activity / cell division site ...lipid-linked peptidoglycan transporter activity / cell septum assembly / peptidoglycan glycosyltransferase / peptidoglycan glycosyltransferase activity / cell septum / serine-type D-Ala-D-Ala carboxypeptidase / FtsZ-dependent cytokinesis / division septum assembly / serine-type D-Ala-D-Ala carboxypeptidase activity / cell division site / penicillin binding / peptidoglycan biosynthetic process / cell wall organization / regulation of cell shape / cell division / proteolysis / plasma membrane
Similarity search - Function
Probable peptidoglycan glycosyltransferase FtsW / Cell division protein FtsL / Cell division protein FtsL / Cell cycle, FtsW / RodA / SpoVE, conserved site / Cell cycle proteins ftsW / rodA / spoVE signature. / Septum formation initiator FtsL/DivIC / Cell division protein FtsB / Septum formation initiator / Cell division protein FtsQ, C-terminal / Cell division protein FtsQ ...Probable peptidoglycan glycosyltransferase FtsW / Cell division protein FtsL / Cell division protein FtsL / Cell cycle, FtsW / RodA / SpoVE, conserved site / Cell cycle proteins ftsW / rodA / spoVE signature. / Septum formation initiator FtsL/DivIC / Cell division protein FtsB / Septum formation initiator / Cell division protein FtsQ, C-terminal / Cell division protein FtsQ / Cell division protein FtsQ/DivIB, C-terminal / POTRA domain, FtsQ-type / Cell division protein FtsQ/DivIB, C-terminal / POTRA domain, FtsQ-type / Probable peptidoglycan glycosyltransferase FtsW/RodA / Cell cycle protein / Peptidoglycan D,D-transpeptidase FtsI / POTRA domain / POTRA domain profile. / 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
Peptidoglycan D,D-transpeptidase FtsI / Cell division protein FtsQ / Cell division protein FtsL / Probable peptidoglycan glycosyltransferase FtsW / Cell division protein FtsB
Similarity search - Component
Biological speciesPseudomonas aeruginosa PAO1 (bacteria)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.8 Å
AuthorsKaeshammer, L. / van den Ent, F. / Jeffery, M. / Lowe, J.
Funding support United Kingdom, 1items
OrganizationGrant numberCountry
Medical Research Council (MRC, United Kingdom) United Kingdom
Citation
Journal: Nat Microbiol / Year: 2023
Title: Cryo-EM structure of the bacterial divisome core complex and antibiotic target FtsWIQBL.
Authors: Lisa Käshammer / Fusinita van den Ent / Magnus Jeffery / Nicolas L Jean / Victoria L Hale / Jan Löwe /
Abstract: In most bacteria, cell division relies on the synthesis of new cell wall material by the multiprotein divisome complex. Thus, at the core of the divisome are the transglycosylase FtsW, which ...In most bacteria, cell division relies on the synthesis of new cell wall material by the multiprotein divisome complex. Thus, at the core of the divisome are the transglycosylase FtsW, which synthesises peptidoglycan strands from its substrate Lipid II, and the transpeptidase FtsI that cross-links these strands to form a mesh, shaping and protecting the bacterial cell. The FtsQ-FtsB-FtsL trimeric complex interacts with the FtsWI complex and is involved in regulating its enzymatic activities; however, the structure of this pentameric complex is unknown. Here, we present the cryogenic electron microscopy structure of the FtsWIQBL complex from Pseudomonas aeruginosa at 3.7 Å resolution. Our work reveals intricate structural details, including an extended coiled coil formed by FtsL and FtsB and the periplasmic interaction site between FtsL and FtsI. Our structure explains the consequences of previously reported mutations and we postulate a possible activation mechanism involving a large conformational change in the periplasmic domain. As FtsWIQBL is central to the divisome, our structure is foundational for the design of future experiments elucidating the precise mechanism of bacterial cell division, an important antibiotic target.
#1: Journal: Nat Microbiol / Year: 2023
Title: Cryo-EM structure of the bacterial divisome core complex and antibiotic target FtsWIQBL.
Authors: Lisa Käshammer / Fusinita van den Ent / Magnus Jeffery / Nicolas L Jean / Victoria L Hale / Jan Löwe /
Abstract: In most bacteria, cell division relies on the synthesis of new cell wall material by the multiprotein divisome complex. Thus, at the core of the divisome are the transglycosylase FtsW, which ...In most bacteria, cell division relies on the synthesis of new cell wall material by the multiprotein divisome complex. Thus, at the core of the divisome are the transglycosylase FtsW, which synthesises peptidoglycan strands from its substrate Lipid II, and the transpeptidase FtsI that cross-links these strands to form a mesh, shaping and protecting the bacterial cell. The FtsQ-FtsB-FtsL trimeric complex interacts with the FtsWI complex and is involved in regulating its enzymatic activities; however, the structure of this pentameric complex is unknown. Here, we present the cryogenic electron microscopy structure of the FtsWIQBL complex from Pseudomonas aeruginosa at 3.7 Å resolution. Our work reveals intricate structural details, including an extended coiled coil formed by FtsL and FtsB and the periplasmic interaction site between FtsL and FtsI. Our structure explains the consequences of previously reported mutations and we postulate a possible activation mechanism involving a large conformational change in the periplasmic domain. As FtsWIQBL is central to the divisome, our structure is foundational for the design of future experiments elucidating the precise mechanism of bacterial cell division, an important antibiotic target.
#2: Journal: Biorxiv / Year: 2022
Title: Divisome core complex in bacterial cell division revealed by cryo-EM
Authors: Kashammer, L. / van den Ent, F. / Jeffery, M. / Jean, N.L. / Hale, V.L. / Lowe, J.
History
DepositionOct 28, 2022Deposition site: PDBE / Processing site: PDBE
Revision 1.0Apr 19, 2023Provider: repository / Type: Initial release
Revision 1.1May 24, 2023Group: Database references / Category: citation / citation_author
Item: _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed ..._citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.identifier_ORCID
Revision 1.2Jun 14, 2023Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation_author.identifier_ORCID

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Probable peptidoglycan glycosyltransferase FtsW
B: Peptidoglycan D,D-transpeptidase FtsI
C: Cell division protein FtsQ
D: Cell division protein FtsL
E: Cell division protein FtsB


Theoretical massNumber of molelcules
Total (without water)166,9115
Polymers166,9115
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_5551
Buried area14360 Å2
ΔGint-99 kcal/mol
Surface area55080 Å2
MethodPISA

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Components

#1: Protein Probable peptidoglycan glycosyltransferase FtsW / PGT / Cell division protein FtsW / Cell wall polymerase / Peptidoglycan polymerase / PG polymerase


Mass: 48241.430 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Pseudomonas aeruginosa PAO1 (bacteria)
Strain: ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1
Gene: ftsW, PA4413 / Production host: Escherichia coli (E. coli)
References: UniProt: Q9HW00, peptidoglycan glycosyltransferase
#2: Protein Peptidoglycan D,D-transpeptidase FtsI / Penicillin-binding protein 3 / PBP-3


Mass: 62933.082 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Pseudomonas aeruginosa PAO1 (bacteria)
Strain: ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1
Gene: ftsI, pbpB, PA4418 / Production host: Escherichia coli (E. coli)
References: UniProt: G3XD46, serine-type D-Ala-D-Ala carboxypeptidase
#3: Protein Cell division protein FtsQ /


Mass: 32290.223 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Pseudomonas aeruginosa PAO1 (bacteria)
Strain: ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1
Gene: ftsQ, PA4409 / Production host: Escherichia coli (E. coli) / References: UniProt: G3XDA7
#4: Protein Cell division protein FtsL /


Mass: 11150.034 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Pseudomonas aeruginosa PAO1 (bacteria)
Strain: ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1
Gene: ftsL, PA4419 / Production host: Escherichia coli (E. coli) / References: UniProt: Q9HVZ6
#5: Protein Cell division protein FtsB /


Mass: 12295.922 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Pseudomonas aeruginosa PAO1 (bacteria)
Strain: ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1
Gene: ftsB, PA3634 / Production host: Escherichia coli (E. coli) / References: UniProt: Q9HXZ6

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: FtsWIQBL / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT
Molecular weightValue: 0.164 MDa / Experimental value: NO
Source (natural)Organism: Pseudomonas aeruginosa PAO1 (bacteria)
Source (recombinant)Organism: Escherichia coli (E. coli) / Strain: C43
Buffer solutionpH: 7
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 3000 nm / Nominal defocus min: 1200 nm
Image recordingElectron dose: 41 e/Å2 / Film or detector model: GATAN K3 (6k x 4k)

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Processing

SoftwareName: PHENIX / Version: 1.19.2_4158: / Classification: refinement
EM software
IDNameVersionCategory
10RELION4initial Euler assignment
11RELION4final Euler assignment
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 3.8 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 136364 / Symmetry type: POINT
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.0039459
ELECTRON MICROSCOPYf_angle_d0.64112824
ELECTRON MICROSCOPYf_dihedral_angle_d4.1851301
ELECTRON MICROSCOPYf_chiral_restr0.0421454
ELECTRON MICROSCOPYf_plane_restr0.0051638

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