+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-45294 | ||||||||||||
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Title | Structure of the human truncated BOS complex in GDN | ||||||||||||
Map data | |||||||||||||
Sample |
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Keywords | membrane protein biogenesis / membrane protein complex / MEMBRANE PROTEIN | ||||||||||||
Function / homology | Function and homology information multi-pass transmembrane protein insertion into ER membrane / multi-pass translocon complex / regulation of protein complex stability / regulation of protein-containing complex assembly / regulation of signal transduction / ribosome binding / carbohydrate binding / membrane => GO:0016020 / protein stabilization / endoplasmic reticulum membrane ...multi-pass transmembrane protein insertion into ER membrane / multi-pass translocon complex / regulation of protein complex stability / regulation of protein-containing complex assembly / regulation of signal transduction / ribosome binding / carbohydrate binding / membrane => GO:0016020 / protein stabilization / endoplasmic reticulum membrane / protein-containing complex / membrane / plasma membrane Similarity search - Function | ||||||||||||
Biological species | Homo sapiens (human) | ||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.65 Å | ||||||||||||
Authors | Nguyen VN / Tomaleri GP / Voorhees RM | ||||||||||||
Funding support | United States, 3 items
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Citation | Journal: To Be Published Title: Role of a holo-insertase complex in the biogenesis of biophysically diverse ER membrane proteins Authors: Page KR / Nguyen VN / Pleiner T / Tomaleri GP / Wang ML / Guna A / Hazu M / Wang T / Chou T / Voorhees RM | ||||||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_45294.map.gz | 175.4 MB | EMDB map data format | |
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Header (meta data) | emd-45294-v30.xml emd-45294.xml | 24.4 KB 24.4 KB | Display Display | EMDB header |
Images | emd_45294.png | 46.3 KB | ||
Filedesc metadata | emd-45294.cif.gz | 7.2 KB | ||
Others | emd_45294_additional_1.map.gz emd_45294_half_map_1.map.gz emd_45294_half_map_2.map.gz | 170.2 MB 318.7 MB 318.7 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-45294 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-45294 | HTTPS FTP |
-Related structure data
Related structure data | 9c7uMC 9c7vC C: citing same article (ref.) M: atomic model generated by this map |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_45294.map.gz / Format: CCP4 / Size: 343 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.832 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Additional map: Original unsharpened map of truncated BOS complex
File | emd_45294_additional_1.map | ||||||||||||
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Annotation | Original unsharpened map of truncated BOS complex | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_45294_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_45294_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Human truncated BOS complex
Entire | Name: Human truncated BOS complex |
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Components |
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-Supramolecule #1: Human truncated BOS complex
Supramolecule | Name: Human truncated BOS complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#3 Details: Human BOS complex of truncated NOMO (delta Ig 1-9), TMEM147, and NCLN |
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Source (natural) | Organism: Homo sapiens (human) |
-Macromolecule #1: Nicalin
Macromolecule | Name: Nicalin / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 63.047145 KDa |
Recombinant expression | Organism: Homo sapiens (human) |
Sequence | String: MLEEAGEVLE NMLKASCLPL GFIVFLPAVL LLVAPPLPAA DAAHEFTVYR MQQYDLQGQP YGTRNAVLNT EARTMAAEVL SRRCVLMRL LDFSYEQYQK ALRQSAGAVV IILPRAMAAV PQDVVRQFME IEPEMLAMET AVPVYFAVED EALLSIYKQT Q AASASQGS ...String: MLEEAGEVLE NMLKASCLPL GFIVFLPAVL LLVAPPLPAA DAAHEFTVYR MQQYDLQGQP YGTRNAVLNT EARTMAAEVL SRRCVLMRL LDFSYEQYQK ALRQSAGAVV IILPRAMAAV PQDVVRQFME IEPEMLAMET AVPVYFAVED EALLSIYKQT Q AASASQGS ASAAEVLLRT ATANGFQMVT SGVQSKAVSD WLIASVEGRL TGLGGEDLPT IVIVAHYDAF GVAPWLSLGA DS NGSGVSV LLELARLFSR LYTYKRTHAA YNLLFFASGG GKFNYQGTKR WLEDNLDHTD SSLLQDNVAF VLCLDTVGRG SSL HLHVSK PPREGTLQHA FLRELETVAA HQFPEVRFSM VHKRINLAED VLAWEHERFA IRRLPAFTLS HLESHRDGQR SSIM DVRSR VDSKTLTRNT RIIAEALTRV IYNLTEKGTP PDMPVFTEQM QIQQEQLDSV MDWLTNQPRA AQLVDKDSTF LSTLE HHLS RYLKDVKQHH VKADKRDPEF VFYDQLKQVM NAYRVKPAVF DLLLAVGIAA YLGMAYVAVQ HFSLLYKTVQ RLLVKA KTQ UniProtKB: Nicalin |
-Macromolecule #2: BOS complex subunit NOMO2
Macromolecule | Name: BOS complex subunit NOMO2 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 42.388957 KDa |
Recombinant expression | Organism: Homo sapiens (human) |
Sequence | String: MLVGQGAGLL GPAVVTAAVV LLLSGVGPAH GSEDIVYALA GVSFEIKAED DQPLPGVLLS LSGGLFRSNL LTQDNGILTF SNLSPGQYY FKPMMKEFRF EPSSQMIEVQ EGQNLKITIT GYRTAYSCYG TVSSLNGEPE QGVAMEAVGQ NDCSIYGEDT V TDEEGKFR ...String: MLVGQGAGLL GPAVVTAAVV LLLSGVGPAH GSEDIVYALA GVSFEIKAED DQPLPGVLLS LSGGLFRSNL LTQDNGILTF SNLSPGQYY FKPMMKEFRF EPSSQMIEVQ EGQNLKITIT GYRTAYSCYG TVSSLNGEPE QGVAMEAVGQ NDCSIYGEDT V TDEEGKFR LRGLLPGCVY HVQLKAEGND HIERALPHHR VIEVGNNDID DVNIIVFRQI NQFDLSGNVI TSSEYLPTLW VK LYKSENL DNPIQTVSLG QSLFFHFPPL LRDGENYVVL LDSTLPRSQY DYILPQVSFT AVGYHKHITL IFNPTRKLPE QDI AQGSYI ALPLTLLVLL AGYNHDKLIP LLLQLTSRLQ GVGALGQAAS DNSGPEDAKR QAKKQKTRRT UniProtKB: BOS complex subunit NOMO2, BOS complex subunit NOMO2 |
-Macromolecule #3: Transmembrane protein 147
Macromolecule | Name: Transmembrane protein 147 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 25.279848 KDa |
Recombinant expression | Organism: Homo sapiens (human) |
Sequence | String: MTLFHFGNCF ALAYFPYFIT YKCSGLSEYN AFWKCVQAGV TYLFVQLCKM LFLATFFPTW EGGIYDFIGE FMKASVDVAD LIGLNLVMS RNAGKGEYKI MVAALGWATA ELIMSRCIPL WVGARGIEFD WKYIQMSIDS NISLVHYIVA SAQVWMITRY D LYHTFRPA ...String: MTLFHFGNCF ALAYFPYFIT YKCSGLSEYN AFWKCVQAGV TYLFVQLCKM LFLATFFPTW EGGIYDFIGE FMKASVDVAD LIGLNLVMS RNAGKGEYKI MVAALGWATA ELIMSRCIPL WVGARGIEFD WKYIQMSIDS NISLVHYIVA SAQVWMITRY D LYHTFRPA VLLLMFLSVY KAFVMETFVH LCSLGSWAAL LARAVVTGLL ALSTLALYVA VVNVHS UniProtKB: Transmembrane protein 147 |
-Macromolecule #4: 2-acetamido-2-deoxy-beta-D-glucopyranose
Macromolecule | Name: 2-acetamido-2-deoxy-beta-D-glucopyranose / type: ligand / ID: 4 / Number of copies: 1 / Formula: NAG |
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Molecular weight | Theoretical: 221.208 Da |
Chemical component information | ChemComp-NAG: |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Concentration | 4 mg/mL | |||||||||||||||||||||
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Buffer | pH: 7.5 Component:
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Vitrification | Cryogen name: ETHANE / Chamber humidity: 95 % / Chamber temperature: 279 K / Instrument: FEI VITROBOT MARK IV | |||||||||||||||||||||
Details | Sample solubilized and purified in GDN. |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Specialist optics | Energy filter - Name: GIF Quantum LS / Energy filter - Slit width: 20 eV |
Image recording | Film or detector model: GATAN K3 (6k x 4k) / Number grids imaged: 1 / Number real images: 15929 / Average electron dose: 60.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: SPOT SCAN / Imaging mode: DARK FIELD / Cs: 2.7 mm / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.0 µm / Nominal magnification: 105000 |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
+Image processing
-Atomic model buiding 1
Initial model |
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Output model | PDB-9c7u: |