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- EMDB-38440: Structure of human 3-methylcrotonyl-CoA carboxylase in complex wi... -

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Basic information

Entry
Database: EMDB / ID: EMD-38440
TitleStructure of human 3-methylcrotonyl-CoA carboxylase in complex with acetyl-CoA (MCC-ACO)
Map data
Sample
  • Complex: Heterododecamer complex of human 3-methylcrotonyl-CoA carboxylase in complex with acetyl-CoA (MCC-ACO)
    • Protein or peptide: Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial
    • Protein or peptide: Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial
  • Ligand: BIOTIN
  • Ligand: ACETYL COENZYME *A
KeywordsBiotin-dependent carboxylase / LIGASE
Function / homology
Function and homology information


3-Methylcrotonyl-CoA carboxylase deficiency / methylcrotonoyl-CoA carboxylase / biotin metabolic process / methylcrotonoyl-CoA carboxylase complex / methylcrotonoyl-CoA carboxylase activity / Defective HLCS causes multiple carboxylase deficiency / Biotin transport and metabolism / L-leucine catabolic process / biotin carboxylase activity / branched-chain amino acid catabolic process ...3-Methylcrotonyl-CoA carboxylase deficiency / methylcrotonoyl-CoA carboxylase / biotin metabolic process / methylcrotonoyl-CoA carboxylase complex / methylcrotonoyl-CoA carboxylase activity / Defective HLCS causes multiple carboxylase deficiency / Biotin transport and metabolism / L-leucine catabolic process / biotin carboxylase activity / branched-chain amino acid catabolic process / Branched-chain amino acid catabolism / coenzyme A metabolic process / biotin binding / mitochondrial matrix / mitochondrion / ATP binding / metal ion binding / cytosol
Similarity search - Function
Methylcrotonoyl-CoA carboxylase beta chain MCCB/AccD1-like / : / Acetyl-coenzyme A carboxyltransferase, C-terminal / Acetyl-coenzyme A (CoA) carboxyltransferase C-terminal domain profile. / Acetyl-coenzyme A carboxyltransferase, N-terminal / Acetyl-coenzyme A (CoA) carboxyltransferase N-terminal domain profile. / Acetyl-CoA carboxylase / Carboxyl transferase domain / Biotin-binding site / Biotin-requiring enzymes attachment site. ...Methylcrotonoyl-CoA carboxylase beta chain MCCB/AccD1-like / : / Acetyl-coenzyme A carboxyltransferase, C-terminal / Acetyl-coenzyme A (CoA) carboxyltransferase C-terminal domain profile. / Acetyl-coenzyme A carboxyltransferase, N-terminal / Acetyl-coenzyme A (CoA) carboxyltransferase N-terminal domain profile. / Acetyl-CoA carboxylase / Carboxyl transferase domain / Biotin-binding site / Biotin-requiring enzymes attachment site. / Biotin carboxylase-like, N-terminal domain / Biotin carboxylase, C-terminal / Biotin carboxylation domain / Biotin carboxylase, N-terminal domain / Biotin carboxylase C-terminal domain / Biotin carboxylation domain profile. / Biotin carboxylase C-terminal domain / Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain / Carbamoyl-phosphate synthase L chain, ATP binding domain / Biotin-requiring enzyme / Rudiment single hybrid motif / Biotinyl/lipoyl domain profile. / Biotin/lipoyl attachment / Single hybrid motif / Pre-ATP-grasp domain superfamily / ATP-grasp fold / ATP-grasp fold profile. / ClpP/crotonase-like domain superfamily / Carbamoyl-phosphate synthase subdomain signature 2.
Similarity search - Domain/homology
Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial / Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.85 Å
AuthorsZhou FY / Zhang YY / Zhou Q / Hu Q
Funding support1 items
OrganizationGrant numberCountry
Not funded
CitationJournal: Elife / Year: 2024
Title: Structural insights into human propionyl-CoA carboxylase (PCC) and 3-methylcrotonyl-CoA carboxylase (MCC)
Authors: Zhou F / Zhang Y / Zhu Y / Zhou Q / Shi Y / Hu Q
History
DepositionDec 25, 2023-
Header (metadata) releaseOct 30, 2024-
Map releaseOct 30, 2024-
UpdateNov 20, 2024-
Current statusNov 20, 2024Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_38440.png

Downloads & links

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Map

FileDownload / File: emd_38440.map.gz / Format: CCP4 / Size: 421.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.08 Å/pix.
x 480 pix.
= 517.104 Å		1.08 Å/pix.
x 480 pix.
= 517.104 Å		1.08 Å/pix.
x 480 pix.
= 517.104 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.0773 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.4
Minimum - Maximum-2.4411352 - 4.6406565
Average (Standard dev.)-0.00010101736 (±0.08861809)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions480480480
Spacing480480480
CellA=B=C: 517.104 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #2

Fileemd_38440_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_38440_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Heterododecamer complex of human 3-methylcrotonyl-CoA carboxylase...

EntireName: Heterododecamer complex of human 3-methylcrotonyl-CoA carboxylase in complex with acetyl-CoA (MCC-ACO)
Components
  • Complex: Heterododecamer complex of human 3-methylcrotonyl-CoA carboxylase in complex with acetyl-CoA (MCC-ACO)
    • Protein or peptide: Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial
    • Protein or peptide: Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial
  • Ligand: BIOTIN
  • Ligand: ACETYL COENZYME *A

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Supramolecule #1: Heterododecamer complex of human 3-methylcrotonyl-CoA carboxylase...

SupramoleculeName: Heterododecamer complex of human 3-methylcrotonyl-CoA carboxylase in complex with acetyl-CoA (MCC-ACO)
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial

MacromoleculeName: Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial
type: protein_or_peptide / ID: 1 / Number of copies: 6 / Enantiomer: LEVO / EC number: methylcrotonoyl-CoA carboxylase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 80.584016 KDa
SequenceString: MAAASAVSVL LVAAERNRWH RLPSLLLPPR TWVWRQRTMK YTTATGRNIT KVLIANRGEI ACRVMRTAKK LGVQTVAVYS EADRNSMHV DMADEAYSIG PAPSQQSYLS MEKIIQVAKT SAAQAIHPGC GFLSENMEFA ELCKQEGIIF IGPPPSAIRD M GIKSTSKS ...String:
MAAASAVSVL LVAAERNRWH RLPSLLLPPR TWVWRQRTMK YTTATGRNIT KVLIANRGEI ACRVMRTAKK LGVQTVAVYS EADRNSMHV DMADEAYSIG PAPSQQSYLS MEKIIQVAKT SAAQAIHPGC GFLSENMEFA ELCKQEGIIF IGPPPSAIRD M GIKSTSKS IMAAAGVPVV EGYHGEDQSD QCLKEHARRI GYPVMIKAVR GGGGKGMRIV RSEQEFQEQL ESARREAKKS FN DDAMLIE KFVDTPRHVE VQVFGDHHGN AVYLFERDCS VQRRHQKIIE EAPAPGIKSE VRKKLGEAAV RAAKAVNYVG AGT VEFIMD SKHNFCFMEM NTRLQVEHPV TEMITGTDLV EWQLRIAAGE KIPLSQEEIT LQGHAFEARI YAEDPSNNFM PVAG PLVHL STPRADPSTR IETGVRQGDE VSVHYDPMIA KLVVWAADRQ AALTKLRYSL RQYNIVGLHT NIDFLLNLSG HPEFE AGNV HTDFIPQHHK QLLLSRKAAA KESLCQAALG LILKEKAMTD TFTLQAHDQF SPFSSSSGRR LNISYTRNMT LKDGKN NVA IAVTYNHDGS YSMQIEDKTF QVLGNLYSEG DCTYLKCSVN GVASKAKLII LENTIYLFSK EGSIEIDIPV PKYLSSV SS QETQGGPLAP MTGTIEKVFV KAGDKVKAGD SLMVMIAMKM EHTIKSPKDG TVKKVFYREG AQANRHTPLV EFEEEESD K RESE

UniProtKB: Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial

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Macromolecule #2: Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial

MacromoleculeName: Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial
type: protein_or_peptide / ID: 2 / Number of copies: 6 / Enantiomer: LEVO / EC number: methylcrotonoyl-CoA carboxylase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 61.406027 KDa
SequenceString: MWAVLRLALR PCARASPAGP RAYHGDSVAS LGTQPDLGSA LYQENYKQMK ALVNQLHERV EHIKLGGGEK ARALHISRGK LLPRERIDN LIDPGSPFLE LSQFAGYQLY DNEEVPGGGI ITGIGRVSGV ECMIIANDAT VKGGAYYPVT VKKQLRAQEI A MQNRLPCI ...String:
MWAVLRLALR PCARASPAGP RAYHGDSVAS LGTQPDLGSA LYQENYKQMK ALVNQLHERV EHIKLGGGEK ARALHISRGK LLPRERIDN LIDPGSPFLE LSQFAGYQLY DNEEVPGGGI ITGIGRVSGV ECMIIANDAT VKGGAYYPVT VKKQLRAQEI A MQNRLPCI YLVDSGGAYL PRQADVFPDR DHFGRTFYNQ AIMSSKNIAQ IAVVMGSCTA GGAYVPAMAD ENIIVRKQGT IF LAGPPLV KAATGEEVSA EDLGGADLHC RKSGVSDHWA LDDHHALHLT RKVVRNLNYQ KKLDVTIEPS EEPLFPADEL YGI VGANLK RSFDVREVIA RIVDGSRFTE FKAFYGDTLV TGFARIFGYP VGIVGNNGVL FSESAKKGTH FVQLCCQRNI PLLF LQNIT GFMVGREYEA EGIAKDGAKM VAAVACAQVP KITLIIGGSY GAGNYGMCGR AYSPRFLYIW PNARISVMGG EQAAN VLAT ITKDQRAREG KQFSSADEAA LKEPIIKKFE EEGNPYYSSA RVWDDGIIDP ADTRLVLGLS FSAALNAPIE KTDFGI FRM

UniProtKB: Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial

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Macromolecule #3: BIOTIN

MacromoleculeName: BIOTIN / type: ligand / ID: 3 / Number of copies: 6 / Formula: BTN
Molecular weightTheoretical: 244.311 Da
Chemical component information

ChemComp-BTN:
BIOTIN

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Macromolecule #4: ACETYL COENZYME *A

MacromoleculeName: ACETYL COENZYME *A / type: ligand / ID: 4 / Number of copies: 6 / Formula: ACO
Molecular weightTheoretical: 809.571 Da
Chemical component information

ChemComp-ACO:
ACETYL COENZYME *A

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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
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.2 µm / Nominal defocus min: 1.2 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.85 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 117900
Initial angle assignmentType: ANGULAR RECONSTITUTION
Final angle assignmentType: ANGULAR RECONSTITUTION

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