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- EMDB-43577: CryoEM Structure of a FtsH Helical Assembly in the Presence of ATP -

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Basic information

Entry
Database: EMDB / ID: EMD-43577
TitleCryoEM Structure of a FtsH Helical Assembly in the Presence of ATP
Map data
Sample
  • Complex: Cryo-EM Structure of FtsH Helical Assembly
    • Protein or peptide: ATP-dependent zinc metalloprotease FtsH
  • Ligand: MAGNESIUM ION
  • Ligand: ZINC ION
  • Ligand: ADENOSINE-5'-TRIPHOSPHATE
Keywordsnucleotide binding / protease / cytoplasmic domain / helical assembly / HYDROLASE
Function / homology
Function and homology information


Hydrolases; Acting on peptide bonds (peptidases); Metalloendopeptidases / ATP-dependent peptidase activity / protein catabolic process / metalloendopeptidase activity / ATP hydrolysis activity / proteolysis / zinc ion binding / ATP binding / identical protein binding / plasma membrane
Similarity search - Function
Peptidase M41, FtsH extracellular / FtsH Extracellular / Peptidase, FtsH / Peptidase M41 / Peptidase M41-like / Peptidase family M41 / AAA ATPase, AAA+ lid domain / AAA+ lid domain / ATPase, AAA-type, conserved site / AAA-protein family signature. ...Peptidase M41, FtsH extracellular / FtsH Extracellular / Peptidase, FtsH / Peptidase M41 / Peptidase M41-like / Peptidase family M41 / AAA ATPase, AAA+ lid domain / AAA+ lid domain / ATPase, AAA-type, conserved site / AAA-protein family signature. / ATPase family associated with various cellular activities (AAA) / ATPase, AAA-type, core / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
ATP-dependent zinc metalloprotease FtsH
Similarity search - Component
Biological speciesThermotoga maritima (bacteria)
Methodhelical reconstruction / cryo EM / Resolution: 2.6 Å
AuthorsLi Y / Zhu J / Zhang Z / Wang F / Egelman EH / Tezcan FA
Funding support United States, 3 items
OrganizationGrant numberCountry
National Science Foundation (NSF, United States)DMR-2004558 United States
Department of Energy (DOE, United States)DE-SC0003844 United States
Department of Energy (DOE, United States)DE-SC0019288 United States
CitationJournal: Nat Chem Biol / Year: 2025
Title: Transforming an ATP-dependent enzyme into a dissipative, self-assembling system.
Authors: Yiying Li / Jie Zhu / Zhiyin Zhang / Jiapeng Wei / Fengbin Wang / Georg Meisl / Tuomas P J Knowles / Edward H Egelman / F Akif Tezcan /
Abstract: Nucleoside triphosphate (NTP)-dependent protein assemblies such as microtubules and actin filaments have inspired the development of diverse chemically fueled molecular machines and active materials ...Nucleoside triphosphate (NTP)-dependent protein assemblies such as microtubules and actin filaments have inspired the development of diverse chemically fueled molecular machines and active materials but their functional sophistication has yet to be matched by design. Given this challenge, we asked whether it is possible to transform a natural adenosine 5'-triphosphate (ATP)-dependent enzyme into a dissipative self-assembling system, thereby altering the structural and functional mode in which chemical energy is used. Here we report that FtsH (filamentous temperature-sensitive protease H), a hexameric ATPase involved in membrane protein degradation, can be readily engineered to form one-dimensional helical nanotubes. FtsH nanotubes require constant energy input to maintain their integrity and degrade over time with the concomitant hydrolysis of ATP, analogous to natural NTP-dependent cytoskeletal assemblies. Yet, in contrast to natural dissipative systems, ATP hydrolysis is catalyzed by free FtsH protomers and FtsH nanotubes serve to conserve ATP, leading to transient assemblies whose lifetimes can be tuned from days to minutes through the inclusion of external ATPases in solution.
History
DepositionJan 31, 2024-
Header (metadata) releaseJan 15, 2025-
Map releaseJan 15, 2025-
UpdateJun 11, 2025-
Current statusJun 11, 2025Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_43577.png

Downloads & links

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Map

FileDownload / File: emd_43577.map.gz / Format: CCP4 / Size: 343 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.86 Å/pix.
x 448 pix.
= 385.28 Å		0.86 Å/pix.
x 448 pix.
= 385.28 Å		0.86 Å/pix.
x 448 pix.
= 385.28 Å

Surface

Projections

Slices (1/3)

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Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.86 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 1.0
Minimum - Maximum-2.2001238 - 6.846802
Average (Standard dev.)0.019894876 (±0.20624933)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions448448448
Spacing448448448
CellA=B=C: 385.28 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #2

Fileemd_43577_half_map_1.map
Projections & Slices
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Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_43577_half_map_2.map
Projections & Slices
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Sample components

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Entire : Cryo-EM Structure of FtsH Helical Assembly

EntireName: Cryo-EM Structure of FtsH Helical Assembly
Components
  • Complex: Cryo-EM Structure of FtsH Helical Assembly
    • Protein or peptide: ATP-dependent zinc metalloprotease FtsH
  • Ligand: MAGNESIUM ION
  • Ligand: ZINC ION
  • Ligand: ADENOSINE-5'-TRIPHOSPHATE

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Supramolecule #1: Cryo-EM Structure of FtsH Helical Assembly

SupramoleculeName: Cryo-EM Structure of FtsH Helical Assembly / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1
Source (natural)Organism: Thermotoga maritima (bacteria)

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Macromolecule #1: ATP-dependent zinc metalloprotease FtsH

MacromoleculeName: ATP-dependent zinc metalloprotease FtsH / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
EC number: Hydrolases; Acting on peptide bonds (peptidases); Metalloendopeptidases
Source (natural)Organism: Thermotoga maritima (bacteria)
Molecular weightTheoretical: 51.493832 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: SGGATMYKPS GNKRVTFKDV GGAEEAIEEL KEVVEFLKDP SKFNRIGARM PKGILLVGPP GTGKTLLARA VAGEANVPFF HISGSDFVE LFVGVGAARV RDLFAQAKAH APSIVFIDEI DAVGRHRGAG LGGGHDEREQ TLNQLLVEMD GFDSKEGIIV M AATNRPDI ...String:
SGGATMYKPS GNKRVTFKDV GGAEEAIEEL KEVVEFLKDP SKFNRIGARM PKGILLVGPP GTGKTLLARA VAGEANVPFF HISGSDFVE LFVGVGAARV RDLFAQAKAH APSIVFIDEI DAVGRHRGAG LGGGHDEREQ TLNQLLVEMD GFDSKEGIIV M AATNRPDI LDPALLRPGR FDKKIVVDPP DMLGRKKILE IHTRNKPLAE DVNLEIIAKR TPGFVGADLE NLVNEAALLA AR EGRDKIT MKDFEEAIDR VIAGPARKSL LISPAEKRII AYHEAGHAVV STVVPNGEPV HRISIIPRGY KALGYTLHLP EED KYLVSR NELLDKLTAL LGGRAAEEVV FGDVTSGAAN DIERATEIAR NMVSQLGMSE ELGPLAWGKE EQEVFLGKEI TRLR NYSEE VASKIDEEVK KIVTNSYERA KEIIRKYRKQ LDNIVEILLE KETIEGDELR RILSEEFEKV VE

UniProtKB: ATP-dependent zinc metalloprotease FtsH

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Macromolecule #2: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 2 / Number of copies: 1 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Macromolecule #3: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 3 / Number of copies: 1 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

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Macromolecule #4: ADENOSINE-5'-TRIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 4 / Number of copies: 1 / Formula: ATP
Molecular weightTheoretical: 507.181 Da
Chemical component information

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

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Experimental details

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Structure determination

Methodcryo EM
Processinghelical reconstruction
Aggregation statehelical array

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Sample preparation

BufferpH: 6
GridModel: Quantifoil R2/1 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: PLASMA CLEANING
VitrificationCryogen name: ETHANE / Chamber humidity: 95 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 70.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.1 µm / Nominal defocus min: 1.5 µm
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Final reconstructionApplied symmetry - Helical parameters - Δz: 9.1 Å
Applied symmetry - Helical parameters - Δ&Phi: 157.5 °
Applied symmetry - Helical parameters - Axial symmetry: C1 (asymmetric)
Resolution.type: BY AUTHOR / Resolution: 2.6 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 840601
CTF correctionType: NONE
Startup modelType of model: PDB ENTRY
PDB model - PDB ID:

3kds

Final angle assignmentType: NOT APPLICABLE
FSC plot (resolution estimation)

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