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- PDB-9cz1: Cryo-EM structure of a 'hat' portion of FtsH.HflK.HflC complex -

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Basic information

Entry
Database: PDB / ID: 9cz1
TitleCryo-EM structure of a 'hat' portion of FtsH.HflK.HflC complex
Components
  • Modulator of FtsH protease HflC
  • Modulator of FtsH protease HflK
KeywordsCHAPERONE / ClpXP / full-engaged state / AAA protease
Function / homology
Function and homology information


peptidase activity / hydrolase activity / cell division / proteolysis / membrane
Similarity search - Function
HflC / HflK / Menbrane protein HflK, N-terminal / Bacterial membrane protein N terminal / : / Stomatin/HflK/HflC family / Band 7 domain / SPFH domain / Band 7 family / prohibitin homologues / Band 7/SPFH domain superfamily
Similarity search - Domain/homology
Modulator of FtsH protease HflC / Protein HflK
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.5 Å
AuthorsGhanbarpour, A. / Sauer, R.T. / Davis, J.H.
Funding support United States, 3items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of Mental Health (NIH/NIMH)R01-GM144542 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R35-GM141517 United States
National Science Foundation (NSF, United States)2046778 United States
CitationJournal: To Be Published
Title: Cryo-EM structure of a 'hat' portion of FtsH.HflK.HflC complex
Authors: Ghanbarpour, A. / Sauer, R.T. / Davis, J.H.
History
DepositionAug 3, 2024Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 13, 2024Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
XA: Modulator of FtsH protease HflK
XB: Modulator of FtsH protease HflC
XC: Modulator of FtsH protease HflK
XD: Modulator of FtsH protease HflC
XE: Modulator of FtsH protease HflK
XF: Modulator of FtsH protease HflC
XG: Modulator of FtsH protease HflK
XH: Modulator of FtsH protease HflC
XI: Modulator of FtsH protease HflK
XJ: Modulator of FtsH protease HflC
XK: Modulator of FtsH protease HflK
XL: Modulator of FtsH protease HflC
XM: Modulator of FtsH protease HflK
XN: Modulator of FtsH protease HflC
XO: Modulator of FtsH protease HflK
XP: Modulator of FtsH protease HflC
XQ: Modulator of FtsH protease HflK
XR: Modulator of FtsH protease HflC
XS: Modulator of FtsH protease HflK
XT: Modulator of FtsH protease HflC
XU: Modulator of FtsH protease HflK
XV: Modulator of FtsH protease HflC
XW: Modulator of FtsH protease HflK
XX: Modulator of FtsH protease HflC


Theoretical massNumber of molelcules
Total (without water)999,63224
Polymers999,63224
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1

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Components

#1: Protein
Modulator of FtsH protease HflK


Mass: 45598.793 Da / Num. of mol.: 12
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli)
Gene: hflK, hflK_1, A8502_001504, ACN81_01545, ACU57_19135, B6R15_002000, B6R31_000826, BANRA_02863, BGM66_001066, BGZ_01593, BGZ_05131, BJI68_16630, BK292_24855, BK383_13095, BTB68_003943, BTQ06_ ...Gene: hflK, hflK_1, A8502_001504, ACN81_01545, ACU57_19135, B6R15_002000, B6R31_000826, BANRA_02863, BGM66_001066, BGZ_01593, BGZ_05131, BJI68_16630, BK292_24855, BK383_13095, BTB68_003943, BTQ06_07290, BvCmsKKP061_03355, BXT93_16385, C0P57_000236, C3F40_14180, CF22_001630, CG704_01810, CIG67_23195, CQ842_09310, CQ842_12110, CTR35_001542, CV83915_01855, D4M65_22455, D9D43_14560, DD762_20800, DIV22_15560, DNQ45_06710, DS732_02655, DTL43_02345, DU321_10415, E2865_05442, E4K51_09085, E5H86_08375, E6D34_03745, EAI46_08375, ECs5150, EIZ93_17475, EN85_000830, EPS97_10200, F7N46_18140, F9461_18000, F9B07_05995, FGAF848_41630, FJQ40_01630, FKO60_18290, FOI11_014740, FOI11_20940, FPS11_03870, FVB16_06380, FWK02_13090, G3V95_10915, G4A38_03090, G4A47_10900, GAI89_04385, GAJ12_10750, GNW61_00325, GOP25_14130, GP965_11000, GP979_12080, GQA06_06275, GQE86_14305, GQM04_15800, GQM21_05505, GQW07_15995, GRO95_15840, GRW05_08865, GRW24_08520, GUC01_09055, H0O53_13460, H0O72_04915, HEP30_009475, HEP34_001782, HHH44_002336, HJQ60_002514, HLZ50_23395, HMV95_06705, HV109_21490, HV209_19960, HVW43_13980, I6H00_16150, I6H02_16705, J0541_002323, J5U05_001376, JNP96_03045, NCTC10082_01824, NCTC10429_04710, NCTC10974_05098, NCTC11181_01756, NCTC11341_03057, NCTC7922_05246, NCTC8500_05052, NCTC8959_04284, NCTC8960_02016, NCTC9044_02658, NCTC9045_05319, NCTC9077_05652, NCTC9117_05600, NCTC9702_05278, NCTC9706_01788, P6223_000677, QDW62_23495, RZR61_04275, SAMEA3472112_03401, SAMEA3752557_01673, WR15_07020
Production host: Escherichia coli (E. coli) / References: UniProt: C3SG32
#2: Protein
Modulator of FtsH protease HflC


Mass: 37703.887 Da / Num. of mol.: 12
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Gene: hflC, NCTC10418_06673 / Production host: Escherichia coli (E. coli) / References: UniProt: A0A376L393
Has protein modificationN

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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: FtsH.HflK.HflKC complex / Type: COMPLEX / Entity ID: all / Source: NATURAL
Molecular weightExperimental value: NO
Source (natural)Organism: Escherichia coli (E. coli) / Strain: BL21
Source (recombinant)Organism: Escherichia coli (E. coli)
Buffer solutionpH: 7.5
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 FIELD / Nominal defocus max: 1750 nm / Nominal defocus min: 50 nm
Image recordingElectron dose: 46.14 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k)

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Processing

EM softwareName: PHENIX / Version: 1.14_3260: / Category: model refinement
CTF correctionDetails: Patch CTF estimation, cryoSPARC / Type: NONE
3D reconstructionResolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 184019 / Symmetry type: POINT

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