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Yorodumi- EMDB-39983: Cryo-EM structure of Mycobacteriophage Douge genome-packed connec... -
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Basic information
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| Title | Cryo-EM structure of Mycobacteriophage Douge genome-packed connector (gp5, gp9, gp10, gp12 and gp13) | |||||||||
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Keywords | Mycobacteriophage / phage structure / Icosahedral / cryo-EM / protein assembly / VIRUS / VIRAL PROTEIN | |||||||||
| Biological species | Mycolicibacterium smegmatis MC2 155 (bacteria) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.74 Å | |||||||||
Authors | Maharana J / Wang CH / Tsai LA / Lowary TL / Ho MC | |||||||||
| Funding support | Taiwan, 2 items
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Citation | Journal: Cell Rep / Year: 2025Title: Cryo-EM and cryo-ET reveal the molecular architecture and host interactions of mycobacteriophage Douge. Authors: Jitendra Maharana / Chun-Hsiung Wang / Li-An Tsai / Yi-Ting Liao / Cheng-Han Yang / Melvin C Shen / Lourriel S Macale / Thang Ngoc Tran / Joemark Narsico / Ronelito J Perez / Sunil Kumar ...Authors: Jitendra Maharana / Chun-Hsiung Wang / Li-An Tsai / Yi-Ting Liao / Cheng-Han Yang / Melvin C Shen / Lourriel S Macale / Thang Ngoc Tran / Joemark Narsico / Ronelito J Perez / Sunil Kumar Tewary / Jian-Li Wu / Hong-You Lin / Shu-Wei Chang / Aaron Franklin / Patrick J Moynihan / Deborah Jacobs-Sera / Krista G Freeman / Graham F Hatfull / Todd L Lowary / Meng-Chiao Ho / ![]() Abstract: Recent reports highlight the efficacy of engineered mycobacteriophages to treat non-tuberculosis mycobacterial disease. Molecular insights into mycobacteriophage architecture and host interactions ...Recent reports highlight the efficacy of engineered mycobacteriophages to treat non-tuberculosis mycobacterial disease. Molecular insights into mycobacteriophage architecture and host interactions could allow structure-guided phage engineering to increase efficacy and broaden host range, but such information is currently unavailable. We describe the cryoelectron microscopy (cryo-EM) structure of mycobacteriophage Douge, which contains 1,105 protein subunits assembled into a complete siphophage and is coated with glycan-binding domains for mycobacterial cell surface interactions. When filled with viral genome, the channel spanning the connector, tail, and baseplate is sealed by tape measure proteins, providing a genome gating system and requiring limited structural changes for genome ejection upon phage-host contact. Nanometer-resolution cryoelectron tomography (cryo-ET) snapshots of phage-host interactions show that the baseplate remains attached to the mycobacterial outer membrane during viral genome ejection. This study reveals high-resolution structural details of this mycobacteriophage and its interaction with host glycans. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_39983.map.gz | 481.6 MB | EMDB map data format | |
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| Header (meta data) | emd-39983-v30.xml emd-39983.xml | 24.2 KB 24.2 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_39983_fsc.xml | 16.9 KB | Display | FSC data file |
| Images | emd_39983.png | 77 KB | ||
| Filedesc metadata | emd-39983.cif.gz | 6.7 KB | ||
| Others | emd_39983_half_map_1.map.gz emd_39983_half_map_2.map.gz | 470.3 MB 470.2 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-39983 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-39983 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 8zdjMC ![]() 8zdhC ![]() 8zdiC ![]() 8zdkC ![]() 8zdlC ![]() 8zdmC ![]() 8zdnC ![]() 8zdoC ![]() 8zdpC ![]() 8zdqC ![]() 8zeaC C: citing same article ( M: atomic model generated by this map |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_39983.map.gz / Format: CCP4 / Size: 512 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: 1.061 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #2
| File | emd_39983_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #1
| File | emd_39983_half_map_2.map | ||||||||||||
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| Density Histograms |
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Sample components
-Entire : Mycolicibacterium smegmatis MC2 155
| Entire | Name: Mycolicibacterium smegmatis MC2 155 (bacteria) |
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| Components |
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-Supramolecule #1: Mycolicibacterium smegmatis MC2 155
| Supramolecule | Name: Mycolicibacterium smegmatis MC2 155 / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / NCBI-ID: 246196 / Sci species name: Mycolicibacterium smegmatis MC2 155 / Virus type: VIRION / Virus isolate: STRAIN / Virus enveloped: No / Virus empty: No |
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-Macromolecule #1: Portal Protein (gp5)
| Macromolecule | Name: Portal Protein (gp5) / type: protein_or_peptide / ID: 1 / Number of copies: 12 / Enantiomer: LEVO |
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| Source (natural) | Organism: Mycolicibacterium smegmatis MC2 155 (bacteria) |
| Molecular weight | Theoretical: 56.662449 KDa |
| Sequence | String: IELPDAISDG EVRKLVENEF WPEFVRRREK LDRIAQWARG EQPDYLIQNA NREKRALLKL AKTPWLGLVV THFTQALFVD GYRAEGSKE NAKGPWQTWN ANKMQSKQIA IHRAALTYGY SYARVLPGVA LDGANQAEIH GVSPRRLLAL YEDQINDEYP K YALELANN ...String: IELPDAISDG EVRKLVENEF WPEFVRRREK LDRIAQWARG EQPDYLIQNA NREKRALLKL AKTPWLGLVV THFTQALFVD GYRAEGSKE NAKGPWQTWN ANKMQSKQIA IHRAALTYGY SYARVLPGVA LDGANQAEIH GVSPRRLLAL YEDQINDEYP K YALELANN GKTVRLYTDT DYYELRMPSP GNFPNEQVIK KVHHGVGVCP FVRYVNMMDL DGFTMGEVEY LVPVASKIDK TD YDRLLAQ HYNSWKVKVA TGIDDLSEDA TPEEQQRAKL ILAQDDILMH GNHEAKFYTL PETSLDGFIA AHTQDVEILA NNA QVPVWI LNGQLANLSA DALTAATKGT IQKLYERQVT FGAAHNQVLR LAAHVEGDTE GARDFTASVS WQDTSVRSLA QAVD AYGKA ATMLGMPKEF LWGLIPGITK TDVEAMRQHF NDDDEMTQML LWWTPNGPGG EFAAEIEVDS QTQIIEAQGD VQKDL QDAQ AKAQADLAKQ NAAAQQRQAV AV |
-Macromolecule #2: Stopper Protein (gp10)
| Macromolecule | Name: Stopper Protein (gp10) / type: protein_or_peptide / ID: 2 / Number of copies: 6 / Enantiomer: LEVO |
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| Source (natural) | Organism: Mycolicibacterium smegmatis MC2 155 (bacteria) |
| Molecular weight | Theoretical: 12.334563 KDa |
| Sequence | String: MNDETLTVYR GATDNKGNPN KQVHGTVKGV FAWGPGTSTN KFGRDRNFKG ESSSLTAELY VKRGADLKAR DRIRRANGEE YSVVGHAAW DQGHPFDGFD FGYMVFQVEA VN |
-Macromolecule #3: Tail Tube Protein (gp13)
| Macromolecule | Name: Tail Tube Protein (gp13) / type: protein_or_peptide / ID: 3 / Number of copies: 6 / Enantiomer: LEVO |
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| Source (natural) | Organism: Mycolicibacterium smegmatis MC2 155 (bacteria) |
| Molecular weight | Theoretical: 31.98083 KDa |
| Sequence | String: TDFYTIKDAQ ADLAIAPLNL TVLLAPYSTT PATTLESPTD GSLAIPPGYK SVGHFEKQAG LTLGNEFDSK DIEAYGEPEP IRTIINKRT TTFDFAMYQN QRNVLELIWT QDFSNIQPSE FGGIVLEAPK VPKNIYYRAI LVGMDDRNDR PIWLYWLMPK V KLDKLDNQ ...String: TDFYTIKDAQ ADLAIAPLNL TVLLAPYSTT PATTLESPTD GSLAIPPGYK SVGHFEKQAG LTLGNEFDSK DIEAYGEPEP IRTIINKRT TTFDFAMYQN QRNVLELIWT QDFSNIQPSE FGGIVLEAPK VPKNIYYRAI LVGMDDRNDR PIWLYWLMPK V KLDKLDNQ TLNDDNVIEY KPTLKAFRDD VVGYSVAQGF AGPGWRDLVA TAGFGEALTA LTITPGSPTV TVATGASHTA QL LVEGDNG INYTPDVVFT SSAPDKASVS AAGLVTGVAA GSATITATKG ALTATATVTV TA |
-Macromolecule #4: Adaptor Protein (gp9)
| Macromolecule | Name: Adaptor Protein (gp9) / type: protein_or_peptide / ID: 4 / Number of copies: 12 / Enantiomer: LEVO |
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| Source (natural) | Organism: Mycolicibacterium smegmatis MC2 155 (bacteria) |
| Molecular weight | Theoretical: 15.174126 KDa |
| Sequence | String: AGLATIDELQ TLMSTVFEDD ALEQAQLVLD IVSSWARVVS GQMWPDAPAN VPDDVRAVVL QASRRELKNP DRVISRQMGP FNVQYSQPP DGFFYPAELA ILKRFKRSGG LMTVSTSRGE EGRPWAGKTA YIRYGDGL |
-Macromolecule #5: Terminator Protein (gp12)
| Macromolecule | Name: Terminator Protein (gp12) / type: protein_or_peptide / ID: 5 / Number of copies: 6 / Enantiomer: LEVO |
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| Source (natural) | Organism: Mycolicibacterium smegmatis MC2 155 (bacteria) |
| Molecular weight | Theoretical: 19.002715 KDa |
| Sequence | String: AVVLPDWYEE AFVNVENLFI DMFTDLLPDY ESGCWAPDDW LADEIEVKPT IWFFRLPGGR VDWDGRKDEC QLQVMVVTGS RDDSWRLMD FVRAMLLPMQ GDKYKMADGY TAQIRCAGEV AGPQLLTPGQ RIDTRVVTAT FKVSVSMKSA KNYKQKLYEL W QALRG |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 7.5 |
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| 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 BIOQUANTUM (6k x 4k) / Average electron dose: 50.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.0 µm / Nominal defocus min: 0.43 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi



Mycolicibacterium smegmatis MC2 155 (bacteria)
Keywords
Authors
Taiwan, 2 items
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Processing
FIELD EMISSION GUN

