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- EMDB-28849: 3-methylcrotonyl-CoA carboxylase in filament, alpha-subunit centered -
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Open data
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Basic information
Entry | ![]() | ||||||||||||||||||||||||
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Title | 3-methylcrotonyl-CoA carboxylase in filament, alpha-subunit centered | ||||||||||||||||||||||||
![]() | mcc | ||||||||||||||||||||||||
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![]() | enzyme / multienzyme / multi-enzyme / biotin-dependent / leucine catabolism / PROTEIN FIBRIL / LIGASE | ||||||||||||||||||||||||
Function / homology | ![]() urea carboxylase activity / propionyl-CoA carboxylase activity / methylcrotonoyl-CoA carboxylase activity / mitochondrion / ATP binding / membrane / metal ion binding Similarity search - Function | ||||||||||||||||||||||||
Biological species | ![]() | ||||||||||||||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.9 Å | ||||||||||||||||||||||||
![]() | Hu JJ / Lee JKJ / Liu YT / Yu C / Huang L / Afasizheva I / Afasizhev R / Zhou ZH | ||||||||||||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Discovery, structure, and function of filamentous 3-methylcrotonyl-CoA carboxylase. Authors: Jason J Hu / Jane K J Lee / Yun-Tao Liu / Clinton Yu / Lan Huang / Inna Aphasizheva / Ruslan Aphasizhev / Z Hong Zhou / ![]() Abstract: 3-methylcrotonyl-CoA carboxylase (MCC) is a biotin-dependent mitochondrial enzyme necessary for leucine catabolism in most organisms. While the crystal structure of recombinant bacterial MCC has been ...3-methylcrotonyl-CoA carboxylase (MCC) is a biotin-dependent mitochondrial enzyme necessary for leucine catabolism in most organisms. While the crystal structure of recombinant bacterial MCC has been characterized, the structure and potential polymerization of native MCC remain elusive. Here, we discovered that native MCC from Leishmania tarentolae (LtMCC) forms filaments, and determined the structures of different filament regions at 3.4, 3.9, and 7.3 Å resolution using cryoEM. αβ LtMCCs assemble in a twisted-stacks architecture, manifesting as supramolecular rods up to 400 nm. Filamentous LtMCCs bind biotin non-covalently and lack coenzyme A. Filaments elongate by stacking αβ LtMCCs onto the exterior α-trimer of the terminal LtMCC. This stacking immobilizes the biotin carboxylase domains, sequestering the enzyme in an inactive state. Our results support a new model for LtMCC catalysis, termed the dual-swinging-domains model, and cast new light on the function of polymerization in the carboxylase superfamily and beyond. | ||||||||||||||||||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 201.9 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 17.9 KB 17.9 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 13.6 KB | Display | ![]() |
Images | ![]() | 62 KB | ||
Filedesc metadata | ![]() | 6.1 KB | ||
Others | ![]() ![]() | 171.6 MB 171.5 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8f41MC ![]() 8f3dC M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
File | ![]() | ||||||||||||||||||||
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Annotation | mcc | ||||||||||||||||||||
Voxel size | X=Y=Z: 1.1 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: h2
File | emd_28849_half_map_1.map | ||||||||||||
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Annotation | h2 | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: h1
File | emd_28849_half_map_2.map | ||||||||||||
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Annotation | h1 | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
-Entire : alpha6beta6 dodecamer in 3-methylcrotonyl-CoA carboxylase filament
Entire | Name: alpha6beta6 dodecamer in 3-methylcrotonyl-CoA carboxylase filament |
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Components |
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-Supramolecule #1: alpha6beta6 dodecamer in 3-methylcrotonyl-CoA carboxylase filament
Supramolecule | Name: alpha6beta6 dodecamer in 3-methylcrotonyl-CoA carboxylase filament type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: 3-methylcrotonyl-CoA carboxylase, beta-subunit
Macromolecule | Name: 3-methylcrotonyl-CoA carboxylase, beta-subunit / type: protein_or_peptide / ID: 1 / Number of copies: 6 / Enantiomer: LEVO / EC number: methylcrotonoyl-CoA carboxylase |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 61.978711 KDa |
Sequence | String: YAHHPIDYER STSKSPNILR LPANTSDPTY QENMARMEGL VEQLRARVRY VQAGGVVPEE EAAKAGVSIS SIEADDRVRK LHLSRGKML ARDRIERLID PGTRFLELSQ LAGWDLYWDD KKKEYERCYS GGIVTGIGLV NGVRCMLVAN DATVKGGTYY P ITVKKHLR ...String: YAHHPIDYER STSKSPNILR LPANTSDPTY QENMARMEGL VEQLRARVRY VQAGGVVPEE EAAKAGVSIS SIEADDRVRK LHLSRGKML ARDRIERLID PGTRFLELSQ LAGWDLYWDD KKKEYERCYS GGIVTGIGLV NGVRCMLVAN DATVKGGTYY P ITVKKHLR AQKIAEQNHL PCIYLVDSGG ANLSRQDDVF PDEQHFGRIF YNEAQMSIKS ISQIAVVMGS CTAGGAYVPA MA DENIIVA RNGTIFLGGP PLVLAATGEK VSSEELGGAD VHCRISGVGD HYATDDLHAL YLARRAVANL NLKEHNEARN PTD VKPVPP LYDPRELGGF IPDMLSDVVK SFDVRAIIAR IVDGSRFDEF KALYGNTLVC GFARIEGMQV GIIANQGILY SESA LKGAH FIGLCTQRNV PLLFLQNITG FMVGKKYEEG GIARNGARLV MAVSSAPVPK VTVLIGGSYG AGNYGMCGRA FEPRF LFMW PNARISVMGG TQAATVLTLT NRNLKNASEA EIAAFKDKVK KKYEKEGSCY YSTARLWDDG VIAPEDTRVV VAEALR ATR LAP |
-Macromolecule #2: 3-methylcrotonyl-CoA carboxylase, alpha-subunit
Macromolecule | Name: 3-methylcrotonyl-CoA carboxylase, alpha-subunit / type: protein_or_peptide / ID: 2 / Number of copies: 6 / Enantiomer: LEVO / EC number: methylcrotonoyl-CoA carboxylase |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 75.103633 KDa |
Sequence | String: ERKVEKLLVA NRGEIACRVF RTCREMHIRT VALFCEAERN AKHVAEADEA VCIGPPPAVN SYLRGEHIIS VAKQLNVDAI HPGYGFLSE NASFADAITR SGIEFIGPPA SAISLMGSKS ESKRIMEAAG VPVVPGYYGE NQNVSFLAEE AKKVGFPILI K AVSGGGGK ...String: ERKVEKLLVA NRGEIACRVF RTCREMHIRT VALFCEAERN AKHVAEADEA VCIGPPPAVN SYLRGEHIIS VAKQLNVDAI HPGYGFLSE NASFADAITR SGIEFIGPPA SAISLMGSKS ESKRIMEAAG VPVVPGYYGE NQNVSFLAEE AKKVGFPILI K AVSGGGGK GMKIVERPED FTFMLESAKR EATNFFKDDR VILERYVKRS RHIECQIFFD KHGRGVFFFE RDCSVQRRYQ KV LEEAPAP HLSMETRQRI GEVALQAAKA VGYVGAGTVE FIFDTSTGEF YFMEMNTRLQ VEHPVTEEVC RIKGAPLDLV KLQ IKTAMG KPLTFSQEDV TLVGSCIEAR VYAESPERGF LPESGPLTFI REPFQGVRGP ARTRLDTGFR EGDNVLIHYD PMLA KVISW GRSREEALRG LRQALGEYKV AGINTNIEFL KRCCETPEFA RGGVTTNFIS EHESQLLKSP VVTPEVAAMA ATAWL LNRC DNWRGAFRLN SDTNATVHFY IDDHPVEVRL HTEGANYHKI FFSVWDHDGS FEVCSGPVTS KHRDQKSIVN DFTFLF ENG MHHTVLAVAT EGDVTVIGSF GLHQLRLLPL TDGFGDSSTA GGTSTKIVSP MPGKVSKLLV KSGDLVEKGQ VLVIVEA MK MEHPVRALQD GRVSFLVKEG EVVGGDHVLA TVAEEE UniProtKB: Methylcrotonoyl-coa carboxylase biotinylated subunitprotein-like protein |
-Macromolecule #3: 5-(HEXAHYDRO-2-OXO-1H-THIENO[3,4-D]IMIDAZOL-6-YL)PENTANAL
Macromolecule | Name: 5-(HEXAHYDRO-2-OXO-1H-THIENO[3,4-D]IMIDAZOL-6-YL)PENTANAL type: ligand / ID: 3 / Number of copies: 6 / Formula: BTI |
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Molecular weight | Theoretical: 228.311 Da |
Chemical component information | ![]() ChemComp-BTI: |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | filament |
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Sample preparation
Buffer | pH: 7.5 |
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Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277.15 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 40.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.5 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
Refinement | Space: REAL / Protocol: AB INITIO MODEL |
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Output model | ![]() PDB-8f41: |