+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-0133 | |||||||||
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Title | Structural snapshots of the Type 9 protein translocon | |||||||||
Map data | Postprocessed EM map for SprA-PorV-PPI complex | |||||||||
Sample |
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Function / homology | Function and homology information chaperone-mediated protein folding / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity Similarity search - Function | |||||||||
Biological species | Flavobacterium johnsoniae (bacteria) / Cytophaga johnsonae (bacteria) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.5 Å | |||||||||
Authors | Deme JC / Lea SM | |||||||||
Funding support | United Kingdom, 2 items
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Citation | Journal: Nature / Year: 2018 Title: Type 9 secretion system structures reveal a new protein transport mechanism. Authors: Frédéric Lauber / Justin C Deme / Susan M Lea / Ben C Berks / Abstract: The type 9 secretion system (T9SS) is the protein export pathway of bacteria of the Gram-negative Fibrobacteres-Chlorobi-Bacteroidetes superphylum and is an essential determinant of pathogenicity in ...The type 9 secretion system (T9SS) is the protein export pathway of bacteria of the Gram-negative Fibrobacteres-Chlorobi-Bacteroidetes superphylum and is an essential determinant of pathogenicity in severe periodontal disease. The central element of the T9SS is a so-far uncharacterized protein-conducting translocon located in the bacterial outer membrane. Here, using cryo-electron microscopy, we provide structural evidence that the translocon is the T9SS protein SprA. SprA forms an extremely large (36-strand) single polypeptide transmembrane β-barrel. The barrel pore is capped on the extracellular end, but has a lateral opening to the external membrane surface. Structures of SprA bound to different components of the T9SS show that partner proteins control access to the lateral opening and to the periplasmic end of the pore. Our results identify a protein transporter with a distinctive architecture that uses an alternating access mechanism in which the two ends of the protein-conducting channel are open at different times. | |||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_0133.map.gz | 96.5 MB | EMDB map data format | |
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Header (meta data) | emd-0133-v30.xml emd-0133.xml | 15.5 KB 15.5 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_0133_fsc.xml | 10.7 KB | Display | FSC data file |
Images | emd_0133.png | 73.2 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-0133 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-0133 | HTTPS FTP |
-Related structure data
Related structure data | 6h3iMC 0134C 6h3jC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_0133.map.gz / Format: CCP4 / Size: 103 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | Postprocessed EM map for SprA-PorV-PPI complex | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.82 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Sample components
-Entire : Complex of SprA, PPI and PorV
Entire | Name: Complex of SprA, PPI and PorV |
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Components |
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-Supramolecule #1: Complex of SprA, PPI and PorV
Supramolecule | Name: Complex of SprA, PPI and PorV / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: Flavobacterium johnsoniae (bacteria) |
Molecular weight | Theoretical: 335 KDa |
-Macromolecule #1: Protein involved in gliding motility SprA
Macromolecule | Name: Protein involved in gliding motility SprA / type: protein_or_peptide / ID: 1 Details: SprA from flavobacterium johnsoniae uniprot Q5I6C7 fjoh_1653 Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Cytophaga johnsonae (bacteria) |
Molecular weight | Theoretical: 270.221688 KDa |
Sequence | String: MRKICIFLLV LFCGNVLRSQ VKPAVQDTTK TQFSVGKMEL ENPPSILSAY KYDPITDRYI YTTSVDGFSI DYPLVLTPKE YEDLLLKES RRDYFRKKMD AIDGKKTGAE AAKKDLLPRY YINSSLFESI FGSNTIDVKP TGSVEMDLGV RYTKQDNPAF S PRNRSSLT ...String: MRKICIFLLV LFCGNVLRSQ VKPAVQDTTK TQFSVGKMEL ENPPSILSAY KYDPITDRYI YTTSVDGFSI DYPLVLTPKE YEDLLLKES RRDYFRKKMD AIDGKKTGAE AAKKDLLPRY YINSSLFESI FGSNTIDVKP TGSVEMDLGV RYTKQDNPAF S PRNRSSLT FDFDQRISMS LMGKIGTRLE VNANYDTQST FAFQNLFKLA YTPSEDDIIQ KVEVGNVSMP LNSTLIRGAQ SL FGVKTQL QFGRTTITGV FSEQKSQTKS VVAENGGTVQ NFDLYALDYD NDRHFFLSQY FRNKYDVSLK NYPFIDSRVQ ITR LEVWVT NKQNRVTTTG GGNNLRNIIA LQDLGEAQVS GVPDNEVVVI SSTAGFFNNP IDSPTSNTNN KYDPATIGQA GSFL NSNIR EIVTAKSGFN NTNVSEATDY SVLENARKLT TNEYTFNPQL GYISLQQRLA NDEILAVAFE YTVGGKVYQV GEFGS DGVD ATVVTGNNSS NQAIITQSLV LKMLKSNLTN VKNPVWNLMM KNVYQIPQAY QIKQDDFRLN ILYTDPSPIN YITPVQ GSS FPPNPAPDSK VEQTPLLNVF NLDRLNYNND PQAGGDGFFD YIPGVTVDVQ NGRVIFTTKE PFGELIFNKL QTGAGES YN DPTTYNANQQ KYVFRNMYRN TQAGALQDSD KNKFLLRGKY KSSGSNGIPI GAFNVPQGSV VVTAAGRVLV EGIDYSVD Y QLGRVQILDP SLQASNTPIE VSLENNSIFG QQTRRFMGFN IEHKISDKFV IGGTYLKMTE RPFTQKSTYG QESVNNTIF GFNGNYSTEV PFLTRLANKL PNIDTDVPSN LSIRGEVAFL RPDAPKASDF QGEATIYVDD FEGSQSTIDM RSAYAWSLAS TPFITSIND NTFNANSNTL EYGFKRAKLS WYTIDPVFYS SKPSGISNDD LSLNTTRRIY SRELYPNTDI AQGQIQVVNT L DLTYYPGE RGPYNNNPSF GASNPSANFG GIMRALNSTN FEQGNVEYIQ FWVLDPYVGN GESPATNAGK IYFNLGEISE DV LKDGRKQ YENGLGPDQV MVNPQPLWGD VPASQSLIYA FDTNPDNRKN QDVGLDGLPS SREGSIYTNY AGEADPAGDD YTY YLNADG GVLERYKNYN GTEGNSAVSI NDPNRGSTTL PDVEDINRDN TMSTINAYYE YSIDVKPGMQ VGENYITDIR EVTN VDLPN GGTTNARWIQ FKIPVSQPQN TIGNITDFRS IRFMRMFMTG FNSQMTVRFG ALDLVRGEWR RYTGTLDAND QNPDD DGVE FDVAAVNIQE NGTKCPVNYV MPPGVQREQL YNNNTVINQN EQALAVRIGG AGLQYQDSRA VFKNVSVDMR QYKKLK MFL HAESLPNQPT LEDDEMVGFI RFGNDFTQNF YQVEIPLKVT KTGGSCSISP DLVWMDDNSI DLALDLLTRM KIKAMSI DI NSSKRDVNGI YYPDNDPDLE GGDGDGKLTL GIKGNPNFGL VRNLMVGVKS RADHKDIKGE VWFNELRLAD LENKGGMA A ILNVDTNMAD FATVSATGRK STIGFGSLEQ GANERDREDV QQYNIVTNLN LGKLLPKKWG INLPFNYAIG EEVITPEYD PFNQDIKLDQ LIRETTDQAE KDNIRTRAID YTKRKSINFI GVRKDRAPEQ KPHVYDIENF TFSQSYNQVE RHDYEVADYE DEQSNSAVN YAYTFQPKEV VPFKSTKFMK KSEYWKLLSD FNFNYLPSNI SFNTNILRQS NRQQFREVEV EGIGLDPLYR R NFAFNYQY GFGFNLTKSL KLNYSATSNN IVRNFLNDDN SPKEDFNIWD DYLDIGTPNQ HAQQLVLNYD IPINKIPIFG FV KASYSYT ADYMWQRSST AFSEYEDPNG TVYDLGNTIQ NSNSNTLTTT LNMNTLYKYL GLTPGAKKTA KPKTAAPPKP GEK IVNTAK PVVSSSPFYD GLIGVLTSIK NVQINYTKNS GTVLPGYTPS VGFLGTSKPS LGFVFGSQDD VRYEAAKRGW LTTY QDFNQ SFTQVSNKLL KVTANIDLLP DLKVDLSMDR SYSENTSEQY SVDPSTNEYK PLSPYTYGMF SISTVMIKTA FSPSD ETQS AAFDDFRSNR LIIANRLAEG HYGSGVAIPR YGDANNPIPA ETDPNYAVYT ANQGYPIGYT KSNQAVLLPA FLAAYT GSD ASSSSTNIFR SFPIPNWSIK YNGLMRYKYF KDKFKRFSLQ HNYRASYTIN QFRSNFDYNS SPKVQDVNTN FYNEIIM SN VNLVEQFSPL IRMDFELKSS LRVLSEIKKD RALSMSFDNN LLTEVKGMEY IIGLGYRFKD VIFSSRLADN PTGIIKSD I NIKADFSLRN NETLVRYLDY DNNQLAAGQN IWSLKLTADY SFSKNLTAIF YYDHSFSKAV ISTSFPLTNI RSGFTLRYN FGN |
-Macromolecule #2: Peptidyl-prolyl cis-trans isomerase
Macromolecule | Name: Peptidyl-prolyl cis-trans isomerase / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO / EC number: peptidylprolyl isomerase |
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Source (natural) | Organism: Cytophaga johnsonae (bacteria) / Strain: ATCC 17061 / DSM 2064 / UW101 |
Molecular weight | Theoretical: 19.219141 KDa |
Sequence | String: MKQLLTALLS LTLFISCSKD KDEVKDYTAE NEKEIVDYLA QNNLTAQRTN SGLYYIITKE GSSESEGENP GEEENTGEGE NTEENENDG HPTLNSNITV IYKGYFTNGK VFDESTEGVS YSLRTLIPGW KEGIPLLKSG GEIQLFVPAH LGYGSNGNKT V PGGAVLIF EITLVSVN |
-Macromolecule #3: PorV
Macromolecule | Name: PorV / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Cytophaga johnsonae (bacteria) / Strain: ATCC 17061 / DSM 2064 / UW101 |
Molecular weight | Theoretical: 44.210043 KDa |
Sequence | String: MKKISLLLIC LLITTFAKAQ DIERPITTGV PFLLVAADAR AAGLGDQGVA TSSDVFSQQW NPAKYAFAED AQGLSISYTP YLTDLANDI SLGQVTYYNK INDRSAFAGS FRYFGFGGIE LRQTGDPNEP TREVNPNEFA LDGSYSLKLS ETFSMAVAAR Y IRSNLKVA ...String: MKKISLLLIC LLITTFAKAQ DIERPITTGV PFLLVAADAR AAGLGDQGVA TSSDVFSQQW NPAKYAFAED AQGLSISYTP YLTDLANDI SLGQVTYYNK INDRSAFAGS FRYFGFGGIE LRQTGDPNEP TREVNPNEFA LDGSYSLKLS ETFSMAVAAR Y IRSNLKVA TEEIDASAAG SFAVDVAGFY QSEEIAYSDF NGRWRAGFNI QNLGPKISYD HDDLSANFLP ANLRVGGGFD FI FDDYNKL GVSLELTKLL VPTPPGPGTP YDANGDGDFT DPGDISQSQA DEANYKKYKD IGWVSGIFKS FGDAPGGFSE ELK EITYSA AAEYMYQDAF AMRLGYYHES PMKGAKQFFS LGAGFKYSMI KVDVSYLFSA SKVKNPLENT LRFSLTFNFG DKYE TY |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.5 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELDBright-field microscopy |
Image recording | Film or detector model: GATAN K2 QUANTUM (4k x 4k) / Detector mode: COUNTING / Average electron dose: 52.0 e/Å2 |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
-Atomic model buiding 1
Refinement | Space: REAL / Protocol: BACKBONE TRACE / Target criteria: Correlation |
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Output model | PDB-6h3i: |