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- EMDB-31633: human Serine beta-lactamase-like protein LACTB truncation variant -

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Basic information

Entry
Database: EMDB / ID: EMD-31633
Titlehuman Serine beta-lactamase-like protein LACTB truncation variant
Map data
Sample
  • Organelle or cellular component: mitochondrial intermembrane space protease truncation
    • Protein or peptide: Serine beta-lactamase-like protein LACTB, mitochondrial
Function / homology
Function and homology information


Hydrolases; Acting on peptide bonds (peptidases) / regulation of lipid metabolic process / lipid metabolic process / peptidase activity / mitochondrion / proteolysis / identical protein binding / cytosol
Similarity search - Function
Beta-lactamase-related / Beta-lactamase / Beta-lactamase/transpeptidase-like
Similarity search - Domain/homology
Serine beta-lactamase-like protein LACTB, mitochondrial
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.08 Å
AuthorsZhang MH / Yang MJ
Funding support China, 1 items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)31671049 China
CitationJournal: Structure / Year: 2022
Title: Structural basis for the catalytic activity of filamentous human serine beta-lactamase-like protein LACTB.
Authors: Minghui Zhang / Laixing Zhang / Runyu Guo / Chun Xiao / Jian Yin / Sensen Zhang / Maojun Yang /
Abstract: Serine beta-lactamase-like protein (LACTB) is a mammalian mitochondrial serine protease that can specifically hydrolyze peptide bonds adjacent to aspartic acid residues and is structurally related to ...Serine beta-lactamase-like protein (LACTB) is a mammalian mitochondrial serine protease that can specifically hydrolyze peptide bonds adjacent to aspartic acid residues and is structurally related to prokaryotic penicillin-binding proteins. Here, we determined the cryoelectron microscopy structures of human LACTB (hLACTB) filaments from wild-type protein, a middle region deletion mutant, and in complex with the inhibitor Z-AAD-CMK at 3.0-, 3.1-, and 2.8-Å resolution, respectively. Structural analysis and activity assays revealed that three interfaces are required for the assembly of hLACTB filaments and that the formation of higher order helical structures facilitates its cleavage activity. Further structural and enzymatic analyses of middle region deletion constructs indicated that, while this region is necessary for substrate hydrolysis, it is not required for filament formation. Moreover, the inhibitor-bound structure showed that hLACTB may cleave peptide bonds adjacent to aspartic acid residues. These findings provide the structural basis underlying hLACTB catalytic activity.
History
DepositionAug 7, 2021-
Header (metadata) releaseFeb 16, 2022-
Map releaseFeb 16, 2022-
UpdateMar 1, 2023-
Current statusMar 1, 2023Processing site: PDBj / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.013
  • Imaged by UCSF Chimera
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  • Surface view colored by cylindrical radius
  • Surface level: 0.013
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-7v21
  • Surface level: 0.013
  • Imaged by UCSF Chimera
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  • Simplified surface model + fitted atomic model
  • Atomic modelsPDB-7v21
  • Imaged by Jmol
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_31633.png

Downloads & links

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Map

FileDownload / File: emd_31633.map.gz / Format: CCP4 / Size: 83.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 0.97 Å
Density
Contour LevelBy AUTHOR: 0.013 / Movie #1: 0.013
Minimum - Maximum-0.049732752 - 0.09179583
Average (Standard dev.)0.00015146984 (±0.0024775898)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin-140-140-140
Dimensions280280280
Spacing280280280
CellA=B=C: 271.6 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z0.970.970.97
M x/y/z280280280
origin x/y/z0.0000.0000.000
length x/y/z271.600271.600271.600
α/β/γ90.00090.00090.000
start NX/NY/NZ535455
NX/NY/NZ134138134
MAP C/R/S123
start NC/NR/NS-140-140-140
NC/NR/NS280280280
D min/max/mean-0.0500.0920.000

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Supplemental data

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Sample components

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Entire : mitochondrial intermembrane space protease truncation

EntireName: mitochondrial intermembrane space protease truncation
Components
  • Organelle or cellular component: mitochondrial intermembrane space protease truncation
    • Protein or peptide: Serine beta-lactamase-like protein LACTB, mitochondrial

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Supramolecule #1: mitochondrial intermembrane space protease truncation

SupramoleculeName: mitochondrial intermembrane space protease truncation / type: organelle_or_cellular_component / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Serine beta-lactamase-like protein LACTB, mitochondrial

MacromoleculeName: Serine beta-lactamase-like protein LACTB, mitochondrial
type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO / EC number: Hydrolases; Acting on peptide bonds (peptidases)
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 47.029566 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: GPAAPAQSPA APDPEASPLA EPPQEQSLAP WSPQTPAPPC SRCFARAIES SRDLLHRIKD EVGAPGIVVG VSVDGKEVWS EGLGYADVE NRVPCKPETV MRIASISKSL TMVALAKLWE AGKLDLDIPV QHYVPEFPEK EYEGEKVSVT TRLLISHLSG I RHYGELYL ...String:
GPAAPAQSPA APDPEASPLA EPPQEQSLAP WSPQTPAPPC SRCFARAIES SRDLLHRIKD EVGAPGIVVG VSVDGKEVWS EGLGYADVE NRVPCKPETV MRIASISKSL TMVALAKLWE AGKLDLDIPV QHYVPEFPEK EYEGEKVSVT TRLLISHLSG I RHYGELYL REKFENSIES LRLFKNDPLF FKPGSQFLYS TFGYTLLAAI VERASGCKYL DYMQKIFHDL DMLTTVQEEN EP VIYNRAR FYVYNKKKRL VNTPYVDNSY KWAGGGFLST VGDLLKFGNA MLYGYQVGLF KNSNENLLPG YLKPETMVMM WTP VPNTEM SWDKEGKYAM AWGVVERKQT YGSCRKQRHY ASHTGGAVGA SSVLLVLPEE LDTETINNKV PPRGIIVSII CNMQ SVGLN STALKIALEF DKDRSD

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.4
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Initial angle assignmentType: ANGULAR RECONSTITUTION
Final angle assignmentType: RANDOM ASSIGNMENT
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.08 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 120786

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