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Open data
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Basic information
Entry | ![]() | ||||||||||||
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Title | Fusobacterium nucleatum BamA-Fab 9 complex | ||||||||||||
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![]() | proteomics / protein folding / membrane protein / structural biology | ||||||||||||
Function / homology | POTRA domain, BamA/TamA-like / Surface antigen variable number repeat / Surface antigen D15-like / POTRA domain / POTRA domain profile. / Bacterial surface antigen (D15) / Omp85 superfamily domain / cell outer membrane / POTRA domain-containing protein![]() | ||||||||||||
Biological species | ![]() | ||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.87 Å | ||||||||||||
![]() | Overly Cottom C / Noinaj N | ||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Characterization of the OMP biogenesis machinery in Fusobacterium nucleatum Authors: Overly Cottom C / Heinz E / Eramilli S / Slade DJ / Kossiakoff A / Noinaj N | ||||||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 230 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 20.4 KB 20.4 KB | Display Display | ![]() |
Images | ![]() | 42 KB | ||
Filedesc metadata | ![]() | 6.4 KB | ||
Others | ![]() ![]() ![]() | 2 MB 226.1 MB 226.1 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 1 MB | Display | ![]() |
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Full document | ![]() | 1 MB | Display | |
Data in XML | ![]() | 15.3 KB | Display | |
Data in CIF | ![]() | 18.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9ccg M: atomic model generated by this map |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Map
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.05 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Additional map: #1
File | emd_45442_additional_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_45442_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_45442_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : FnBamA-Fab9 complex
Entire | Name: FnBamA-Fab9 complex |
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Components |
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-Supramolecule #1: FnBamA-Fab9 complex
Supramolecule | Name: FnBamA-Fab9 complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 121 kDa/nm |
-Macromolecule #1: POTRA domain-containing protein
Macromolecule | Name: POTRA domain-containing protein / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 75.980375 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: LPIKSVEVVN NQQVPASLIK NTLKLKEGAK FSTEALLADF NALKETGYFE DVILQPVSYD GGVRIVVDVV EKENVVDLLK EKGVAINTL REDTDKSIVL SSVKFTGNKR VTTSELLDIT QLKAGEYFSR SRVEDAQRRL LATGKFSEVR PDAQVANGKM A LSFEVVEN ...String: LPIKSVEVVN NQQVPASLIK NTLKLKEGAK FSTEALLADF NALKETGYFE DVILQPVSYD GGVRIVVDVV EKENVVDLLK EKGVAINTL REDTDKSIVL SSVKFTGNKR VTTSELLDIT QLKAGEYFSR SRVEDAQRRL LATGKFSEVR PDAQVANGKM A LSFEVVEN PIVKSVIITG NNTIPTSTIM SELTTKPGSV QNYNNLREDR DKILGLYQAQ GYTLVNITDM STDENGTLHI SI VEGIVRR IEVKKMVTKQ KGNRRTPNDD VLKTKDYVID REIEIQPGKI FNVKEYDATV DNLMRLGIFK NVKYEARSIP GDP EGIDLI LLIDEDRTAE LQGGVAYGSE TGFLGTLSLK DSNWRGKNQQ FGFTFEKSNK NYTGFALDFY DPWIKDTDRV SWGW GAYRT SYGDEDSILF HEIDTIGFRT NIGKGLGKNF TLSLGTKVEY IKEKHEDGKL RQANNGKWYY KEKNKWREIE GVDDK YWLW SIYPYISYDT RNNYLNPTSG FYGKFQVEAG HAGGYKSGNF GNATLELRTY HKGLFKNNIF AYKVVGGVAT NNTKES QKF WVGGGNSLRG YDGGFFKGSQ KLVATIENRT QLNDIIGLVV FADAGRAWKQ NGRDPSYTRD NSRFGHNIGT TAGVGIR LN TPIGPLRFDF GWPVGNKMDD DGMKFYFNMG QSF UniProtKB: POTRA domain-containing protein |
-Macromolecule #2: Fab 9 heavy chain
Macromolecule | Name: Fab 9 heavy chain / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: synthetic construct (others) |
Molecular weight | Theoretical: 24.276992 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: EVQLVESGGG LVQPGGSLRL SCAASGFNVY SSSIHWVRQA PGKGLEWVAS IYSYYGSTYY ADSVKGRFTI SADTSKNTAY LQMNSLRAE DTAVYYCARG YSSYWLKSHQ WPYGFDYWGQ GTLVTVSSAS TKGPSVFPLA PSSKSTSGGT AALGCLVKDY F PEPVTVSW ...String: EVQLVESGGG LVQPGGSLRL SCAASGFNVY SSSIHWVRQA PGKGLEWVAS IYSYYGSTYY ADSVKGRFTI SADTSKNTAY LQMNSLRAE DTAVYYCARG YSSYWLKSHQ WPYGFDYWGQ GTLVTVSSAS TKGPSVFPLA PSSKSTSGGT AALGCLVKDY F PEPVTVSW NSGALTSGVH TFPAVLQSSG LYSLSSVVTV PSSSLGTQTY ICNVNHKPSN TKVDKKVEP |
-Macromolecule #3: Fab 9 light chain
Macromolecule | Name: Fab 9 light chain / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: synthetic construct (others) |
Molecular weight | Theoretical: 23.100695 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: QMTQSPSSLS ASVGDRVTIT CRASQSVSSA VAWYQQKPGK APKLLIYSAS SLYSGVPSRF SGSRSGTDFT LTISSLQPED FATYYCQQF SQRLVTFGQG TKVEIKRTVA APSVFIFPPS DSQLKSGTAS VVCLLNNFYP REAKVQWKVD NALQSGNSQE S VTEQDSKD ...String: QMTQSPSSLS ASVGDRVTIT CRASQSVSSA VAWYQQKPGK APKLLIYSAS SLYSGVPSRF SGSRSGTDFT LTISSLQPED FATYYCQQF SQRLVTFGQG TKVEIKRTVA APSVFIFPPS DSQLKSGTAS VVCLLNNFYP REAKVQWKVD NALQSGNSQE S VTEQDSKD STYSLSSTLT LSKADYEKHK VYACEVTHQG LSSPVTKSFN RGEC |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.4 Component:
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Vitrification | Cryogen name: ETHANE | |||||||||
Details | This sample was monodisperse |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 57.8 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.6 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |