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Yorodumi- EMDB-55148: Cryo-EM density map of essential Mycoplasma pneumoniae lipoprotei... -
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Open data
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Basic information
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| Title | Cryo-EM density map of essential Mycoplasma pneumoniae lipoprotein Mpn436 at 3.65 A | |||||||||
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Sample |
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Keywords | PPIase Chaperone Mycoplasma pneumoniae lipoprotein / CHAPERONE | |||||||||
| Function / homology | Protein of unknown function DUF3713 / Protein of unknown function (DUF3713) / Prokaryotic membrane lipoprotein lipid attachment site profile. / plasma membrane / Uncharacterized lipoprotein MG307 homolog Function and homology information | |||||||||
| Biological species | Mycoplasmoides pneumoniae M129 (bacteria) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.65 Å | |||||||||
Authors | Manger S / Keles I | |||||||||
| Funding support | Germany, 1 items
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Citation | Journal: To Be PublishedTitle: Structures of the essential Mycoplasma pneumoniae lipoproteins Mpn444 and Mpn436 reveal a peptidyl-prolyl isomerase domain involved in extracellular protein folding Authors: Manger S / Keles I / Frangakis AS / Scheffer MP / Mantanya MS | |||||||||
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_55148.map.gz | 382.7 MB | EMDB map data format | |
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| Header (meta data) | emd-55148-v30.xml emd-55148.xml | 15.9 KB 15.9 KB | Display Display | EMDB header |
| Images | emd_55148.png | 48.4 KB | ||
| Filedesc metadata | emd-55148.cif.gz | 6.9 KB | ||
| Archive directory | https://data.pdbj.org/pub/emdb/structures/EMD-55148 ftp://data.pdbj.org/pub/emdb/structures/EMD-55148 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9srrMC ![]() 9srvMC ![]() 9srqC ![]() 9srsC ![]() 9sscC C: citing same article ( M: atomic model generated by this map |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_55148.map.gz / Format: CCP4 / Size: 421.9 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: 0.92 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
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Sample components
-Entire : Essential Mycoplasma pneumoniae lipoprotein Mpn436
| Entire | Name: Essential Mycoplasma pneumoniae lipoprotein Mpn436 |
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| Components |
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-Supramolecule #1: Essential Mycoplasma pneumoniae lipoprotein Mpn436
| Supramolecule | Name: Essential Mycoplasma pneumoniae lipoprotein Mpn436 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all Details: Recombinantly expressed in E. coli without the N-terminal signal peptide |
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| Source (natural) | Organism: Mycoplasmoides pneumoniae M129 (bacteria) |
| Molecular weight | Theoretical: 145 KDa |
-Macromolecule #1: Uncharacterized lipoprotein MG307 homolog
| Macromolecule | Name: Uncharacterized lipoprotein MG307 homolog / type: protein_or_peptide / ID: 1 Details: Full-length protein without the N-terminal signal peptide Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: Mycoplasmoides pneumoniae M129 (bacteria) |
| Molecular weight | Theoretical: 139.269438 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MKKFLRKPQF WLLTLGGFLS TSVILAACAT PSNSALQTVF KARSSQFFNG EQGSLQSALT TALKNPVANK QFIAAPLLKA LEAWYENNE DKKITQFLKD TKSNVDSQYT TAVDKVVSAS RNKSLFVQQD LLDNAGGSEA TWKAQKLLEQ LISDFASRVF Q KNYLNYKK ...String: MKKFLRKPQF WLLTLGGFLS TSVILAACAT PSNSALQTVF KARSSQFFNG EQGSLQSALT TALKNPVANK QFIAAPLLKA LEAWYENNE DKKITQFLKD TKSNVDSQYT TAVDKVVSAS RNKSLFVQQD LLDNAGGSEA TWKAQKLLEQ LISDFASRVF Q KNYLNYKK DGQVSTGPFT YDELHKEESW KNFEFSAPRF SETNDDFFAK IQSQVFDQWV EYTDPTLISQ VNYKYSAPSQ GL GQIYNRE KLKDKLTPSY AFPFFAEEKD IAPNQNVGNK RWKQLVKGEG AITDNNIGQS GTNSQKTGLL KYRNESNKGD FLD FPLNLS DTNETKQLVD ASNIVDQLEA ANLGAALNLK LQVFEQDNDE LPQIKELKED LNNTIVVDKS KDVEKASKTN ALFY NDQEG KQQQSDSDPI AGALDDIFAQ NTSEGTNLSK LAEQVKKAAA TKMEAKTAVL RTNNSKGQQN NYVVLDAAIP TFNST TSKS KNNSASNEVL VALKSGSINL RQVQQTDQNS YSPIKFRIVR NSTGVTVFGL DGGSYYLKQD STNKKSVSKQ SLTLLT KSS SGNSNKVLRD LDKQKQFLKF RAFQAKTNTF YSTNFAFSFP LNETLKSWFD KHRELILANA LVNASLDQKD KASKALT EA FNPYKELIKE FAPVALATTM ISFYFDQMKA LNNKLLERAR NLNQNVNQAN PTPWLNGLSA KLPYVNTNGN YEKLNNYF T FLITKTLWPK VGQEETSISE ESNKLKTKTA DVDKIRDKIL ENIQTKVNDF VKNKLKPALA PRPAYSNVIL LNVNNDKVL SSGANWSLAS LLQSDKVNPL SFMLLKQAFD NNDLFKKAQK LFKDIQEKSS NNGGMQSSST TNSDADALSK VIGNYYYTTW AKLTDKSIY GNPKDNKFDE LFKLAFEASI DEKSFNVDYK AVIDHYRFIY TLQWLVDQKL KNFKSLLKTN LKFGEVAFIA Y KNTETTNF SNPQGVFGSY FNYENSASEV KESTQTLDPN NFFYKTTTKP TVQAIQQVAS LALVQKQQMQ QNSTDHYGFT GL STSTSSM FDASSRDAIL QQITKTSLQQ YGSKDQLKKI IQGTNNQLLL DRIAVQLSGL NPSTTNGGSG KTIATYFQVD AVG NPTLDF QAKRKLLLDL LDQYQNYFGN GAQKSQRDST PSGTGNYLTY QNGSDKYTYT QFTYQDIDSL SLTTTSGTNN KIAS DVVAA LLLFQAADKG TQQLALSAIN KPQLNIGDKR IESGLKLLK UniProtKB: Uncharacterized lipoprotein MG307 homolog |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Concentration | 0.8 mg/mL |
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| Buffer | pH: 7.4 Details: 20 mM Tris pH 7.4, 200 mM NaCl and 0 to 0.01% LMNG or 1 mM CHAPSO |
| Grid | Model: C-flat-1.2/1.3 / Material: COPPER / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 45 sec. |
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 278 K / Instrument: FEI VITROBOT MARK IV Details: Nominal blot force -3 Wait time 10 s Blotting time 8 to 14 s. Before freezing, Whatman 595 filter papers were incubated for 1 h in the Vitrobot chamber at 100% relative humidity and 278K.. |
| Details | Concentration range from 0.5 mg/ml to 0.8 mg/ml |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Specialist optics | Energy filter - Name: GIF Quantum SE / Energy filter - Slit width: 20 eV |
| Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2 Details: The camera was operated in dose-fractionation counting mode with a dose rate of ~16 electrons per A2 s-1, resulting in a total dose of 50 electrons per A2. The frame time was adjusted to 1 ...Details: The camera was operated in dose-fractionation counting mode with a dose rate of ~16 electrons per A2 s-1, resulting in a total dose of 50 electrons per A2. The frame time was adjusted to 1 frame per 1 electron per A2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | C2 aperture diameter: 70.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 3.6 µm / Nominal defocus min: 0.8 µm / Nominal magnification: 105000 |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
| Initial model | Chain - Source name: AlphaFold / Chain - Initial model type: in silico model |
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| Refinement | Protocol: AB INITIO MODEL |
| Output model | ![]() PDB-9srr: ![]() PDB-9srv: |
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Keywords
Mycoplasmoides pneumoniae M129 (bacteria)
Authors
Germany, 1 items
Citation












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FIELD EMISSION GUN
