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- EMDB-30986: Cryo-EM structure of the yeast mitochondrial SAM-Tom40/Tom5/Tom6 ... -
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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-30986 | |||||||||
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Title | Cryo-EM structure of the yeast mitochondrial SAM-Tom40/Tom5/Tom6 complex at 3.0 angstrom | |||||||||
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![]() | TRANSLOCASE | |||||||||
Function / homology | ![]() mitochondrial outer membrane translocase complex assembly / SAM complex / membrane insertase activity / mitochondrial outer membrane translocase complex / mitochondrial respiratory chain complex assembly / protein import into mitochondrial matrix / phospholipid transport / protein targeting to mitochondrion / protein insertion into mitochondrial outer membrane / porin activity ...mitochondrial outer membrane translocase complex assembly / SAM complex / membrane insertase activity / mitochondrial outer membrane translocase complex / mitochondrial respiratory chain complex assembly / protein import into mitochondrial matrix / phospholipid transport / protein targeting to mitochondrion / protein insertion into mitochondrial outer membrane / porin activity / pore complex / protein transmembrane transporter activity / monoatomic ion transport / mitochondrion organization / mitochondrial intermembrane space / protein-containing complex assembly / mitochondrial outer membrane / mitochondrion / cytoplasm / cytosol Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.05 Å | |||||||||
![]() | Wang Q / Guan ZY | |||||||||
![]() | ![]() Title: Structural insight into the SAM-mediated assembly of the mitochondrial TOM core complex. Authors: Qiang Wang / Zeyuan Guan / Liangbo Qi / Jinjin Zhuang / Chen Wang / Sixing Hong / Ling Yan / Yan Wu / Xiaoqian Cao / Jianbo Cao / Junjie Yan / Tingting Zou / Zhu Liu / Delin Zhang / Chuangye Yan / Ping Yin / ![]() Abstract: β barrel outer membrane proteins (β-OMPs) play vital roles in mitochondria, chloroplasts, and Gram-negative bacteria. Evolutionarily conserved complexes such as the mitochondrial sorting and ...β barrel outer membrane proteins (β-OMPs) play vital roles in mitochondria, chloroplasts, and Gram-negative bacteria. Evolutionarily conserved complexes such as the mitochondrial sorting and assembly machinery (SAM) mediate the assembly of β-OMPs. We investigated the SAM-mediated assembly of the translocase of the outer membrane (TOM) core complex. Cryo–electron microscopy structures of SAM–fully folded Tom40 and the SAM-Tom40/Tom5/Tom6 complexes at ~3-angstrom resolution reveal that Sam37 stabilizes the mature Tom40 mainly through electrostatic interactions, thus facilitating subsequent TOM assembly. These results support the β barrel switching model and provide structural insights into the assembly and release of β barrel complexes. | |||||||||
History |
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Structure visualization
Movie |
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 78.9 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 18.5 KB 18.5 KB | Display Display | ![]() |
Images | ![]() | 92.1 KB | ||
Filedesc metadata | ![]() | 6.4 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 476.7 KB | Display | ![]() |
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Full document | ![]() | 476.3 KB | Display | |
Data in XML | ![]() | 6.3 KB | Display | |
Data in CIF | ![]() | 7.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7e4iMC ![]() 7e4hC C: citing same article ( M: atomic model generated by this map |
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Similar structure data |
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Links
EMDB pages | ![]() ![]() |
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Map
File | ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Voxel size | X=Y=Z: 1.087 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
-Entire : SAM-Tom40/Tom5/Tom6 complex
Entire | Name: SAM-Tom40/Tom5/Tom6 complex |
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Components |
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-Supramolecule #1: SAM-Tom40/Tom5/Tom6 complex
Supramolecule | Name: SAM-Tom40/Tom5/Tom6 complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() ![]() |
-Supramolecule #2: Sorting assembly machinery subunits
Supramolecule | Name: Sorting assembly machinery subunits / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1-#3 |
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Source (natural) | Organism: ![]() ![]() |
-Supramolecule #3: Mitochondrial import receptor subunits
Supramolecule | Name: Mitochondrial import receptor subunits / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #4-#6 |
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-Macromolecule #1: Sorting assembly machinery 50 kDa subunit
Macromolecule | Name: Sorting assembly machinery 50 kDa subunit / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 54.544918 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MATSSSGVDN EISLDSPMPI FNESSTLKPI RVAGVVTTGT DHIDPSVLQA YLDDTIMKSI TLGQLVKNAD VLNKRLCQHH IALNAKQSF HFQGNTYISD EKETHDVVPL MEVVSQLDIL PPKTFTAKTG TNFGNDNDAE AYLQFEKLID KKYLKLPTRV N LEILRGTK ...String: MATSSSGVDN EISLDSPMPI FNESSTLKPI RVAGVVTTGT DHIDPSVLQA YLDDTIMKSI TLGQLVKNAD VLNKRLCQHH IALNAKQSF HFQGNTYISD EKETHDVVPL MEVVSQLDIL PPKTFTAKTG TNFGNDNDAE AYLQFEKLID KKYLKLPTRV N LEILRGTK IHSSFLFNSY SSLSPQSILN LKVFSQFYNW NTNKGLDIGQ RGARLSLRYE PLFLHKLLHN PHSNESPTLF HE WFLETCW RSTKICSQGT SAPYMYSGTM LSQAGDQLRT ILGHTFVLDK RDHIMCPTKG SMLKWSNELS PGKHLKTQLE LNS VKSWMN DDFITFSTTI KTGYLKNLSS QQSLPVHICD KFQSGGPSDI RGFQTFGLGP RDLYDAVGGD AFVSYGLSVF SRLP WKKVE KSNFRLHWFF NGGKLVNHDN TSLGNCIGQL SKEHSTSTGI GLVLRHPMAR FELNFTLPIT AHENDLIRKG FQFGL GLAF L UniProtKB: Sorting assembly machinery 50 kDa subunit |
-Macromolecule #2: Sorting assembly machinery 35 kDa subunit
Macromolecule | Name: Sorting assembly machinery 35 kDa subunit / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 37.44607 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MVSSFSVPMP VKRIFDTFPL QTYAAQTDKD EAVALEIQRR SYTFTERGGG SSELTVEGTY KLGVYNVFLE ANTGAALATD PWCLFVQLA LCQKNGLVLP THSQEQTPSH TCNHEMLVLS RLSNPDEALP ILVEGYKKRI IRSTVAISEI MRSRILDDAE Q LMYYTLLD ...String: MVSSFSVPMP VKRIFDTFPL QTYAAQTDKD EAVALEIQRR SYTFTERGGG SSELTVEGTY KLGVYNVFLE ANTGAALATD PWCLFVQLA LCQKNGLVLP THSQEQTPSH TCNHEMLVLS RLSNPDEALP ILVEGYKKRI IRSTVAISEI MRSRILDDAE Q LMYYTLLD TVLYDCWITQ IIFCASDAQF MELYSCQKLS GSIVTPLDVE NSLLQKLSAK SLKISLTKRN KFQFRHREIV KS MQGVYHN HHNSVNQEQV LNVLFENSKQ VLLGLKDMLK SDGQPTYLHL KIASYILCIT NVKEPIKLKT FVENECKELV QFA QDTLKN FVQ UniProtKB: Sorting assembly machinery 35 kDa subunit |
-Macromolecule #3: Sorting assembly machinery 37 kDa subunit
Macromolecule | Name: Sorting assembly machinery 37 kDa subunit / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 40.498754 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MVKGSVHLWG KDGKASLISV DSIALVWFIK LCTSEEAKSM VAGLQIVFSN NTDLSSDGKL PVLILDNGTK VSGYVNIVQF LHKNICTSK YEKGTDYEED LAIVRKKDRL LEYSLLNYVD VEISRLTDYQ LFLNTKNYNE YTKKLFSKLL YFPMWYNTPL Q LRSQAREN ...String: MVKGSVHLWG KDGKASLISV DSIALVWFIK LCTSEEAKSM VAGLQIVFSN NTDLSSDGKL PVLILDNGTK VSGYVNIVQF LHKNICTSK YEKGTDYEED LAIVRKKDRL LEYSLLNYVD VEISRLTDYQ LFLNTKNYNE YTKKLFSKLL YFPMWYNTPL Q LRSQAREN CEEIIGSLTL EDDEEFVESK AMESASQLAQ SKTFKIAHKN KIKGKQELQQ VKYNLQFDNR LQSCVSNWLA AR KKLDDSV ILSSDLLFLA NLYVQLGLPD GNRIRSKLEQ TFGSELLNSM SNKIDDFVHR PSNNLEQRDP QFREQGNVVM SLY NLACKY ILEDYKDHDG DYKDHDIDYK DDDDK UniProtKB: Sorting assembly machinery 37 kDa subunit |
-Macromolecule #4: Mitochondrial import receptor subunit TOM40
Macromolecule | Name: Mitochondrial import receptor subunit TOM40 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 43.947262 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MASAPTPLAE ASQIPTIPAL SPLTAKQSKG NFFSSNPISS FVVDTYKQLH SHRQSLELVN PGTVENLNKE VSRDVFLSQY FFTGLRADL NKAFSMNPAF QTSHTFSIGS QALPKYAFSA LFANDNLFAQ GNIDNDLSVS GRLNYGWDKK NISKVNLQIS D GQPTMCQL ...String: MASAPTPLAE ASQIPTIPAL SPLTAKQSKG NFFSSNPISS FVVDTYKQLH SHRQSLELVN PGTVENLNKE VSRDVFLSQY FFTGLRADL NKAFSMNPAF QTSHTFSIGS QALPKYAFSA LFANDNLFAQ GNIDNDLSVS GRLNYGWDKK NISKVNLQIS D GQPTMCQL EQDYQASDFS VNVKTLNPSF SEKGEFTGVA VASFLQSVTP QLALGLETLY SRTDGSAPGD AGVSYLTRYV SK KQDWIFS GQLQANGALI ASLWRKVAQN VEAGIETTLQ AGMVPITDPL MGTPIGIQPT VEGSTTIGAK YEYRQSVYRG TLD SNGKVA CFLERKVLPT LSVLFCGEID HFKNDTKIGC GLQFETAGNQ ELLMLQQGLD ADGNPLQALP QLLESAGKPI PNPL LGLDS T UniProtKB: Mitochondrial import receptor subunit TOM40 |
-Macromolecule #5: Mitochondrial import receptor subunit TOM5
Macromolecule | Name: Mitochondrial import receptor subunit TOM5 / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 6.196197 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MAMFGLPQQE VSEEEKRAHQ EQTEKTLKQA AYVAAFLWVS PMIWHLVKKQ WK UniProtKB: Mitochondrial import receptor subunit TOM5 |
-Macromolecule #6: Mitochondrial import receptor subunit TOM6
Macromolecule | Name: Mitochondrial import receptor subunit TOM6 / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 6.481539 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MADGMFAMPG AAAGAASPQQ PKSRFQAFKE SPLYTIALNG AFFVAGVAFI QSPLMDMLAP QL UniProtKB: Mitochondrial import receptor subunit TOM6 |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Concentration | 6 mg/mL |
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Buffer | pH: 7.4 |
Vitrification | Cryogen name: ETHANE |
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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: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Startup model | Type of model: RANDOM CONICAL TILT |
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Final reconstruction | Applied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.05 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 3.0) / Number images used: 406531 |
Initial angle assignment | Type: PROJECTION MATCHING |
Final angle assignment | Type: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 3.0) |