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- EMDB-61588: Cryo-EM Structure of Bacteriophage FCWL1 head-to-tail interface -
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Open data
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Basic information
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Title | Cryo-EM Structure of Bacteriophage FCWL1 head-to-tail interface | |||||||||
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![]() | T1-like phage / neck / tail / VIRAL PROTEIN | |||||||||
Function / homology | ![]() Phage tail tube protein 3 / Phage tail tube protein, TTP / Protein of unknown function DUF4128 / Phage tail terminator protein / Protein of unknown function DUF4054 / Protein of unknown function (DUF4054) / Protein of unknown function DUF1073 / Phage portal protein Similarity search - Domain/homology | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.3 Å | |||||||||
![]() | Cai C / Wang Y / Liu Y / Shao Q / Wang A / Fang Q / Zheng Y / Zhang T / Luo Z / Yang C | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Structures of a T1-like siphophage reveal capsid stabilization mechanisms and high structural similarities with a myophage. Authors: Can Cai / Yueting Wang / Yunshu Liu / Qianqian Shao / Aohan Wang / Lin Li / Yaqi Zheng / Tianyi Zhang / Ziwen Luo / Chongguang Yang / Qianglin Fang / ![]() Abstract: Bacteriophage T1, a member of Siphoviruses, infects Escherichia coli with high efficiency, making it a promising candidate for phage therapy. Here, we report the near-atomic structures of FCWL1, a T1- ...Bacteriophage T1, a member of Siphoviruses, infects Escherichia coli with high efficiency, making it a promising candidate for phage therapy. Here, we report the near-atomic structures of FCWL1, a T1-like phage that belongs to the T1 phage family. We focus on the head, the head-to-tail interface, and its surrounding components. The hexameric capsomer displays unique gaps between neighboring A domains of the major capsid proteins. These gaps are partially filled by the N-loop of the decoration protein, which adopts a unique conformation. These structural features suggest that the phage might employ a novel strategy for stabilizing its head. Furthermore, despite being a siphophage, the head and head-to-tail connector of the phage show high structural similarity to those of a myophage. These findings enhance our understanding of the structure, capsid stabilization mechanism, and evolution of phages in the T1 family. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 228.8 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 21.2 KB 21.2 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 14.1 KB | Display | ![]() |
Images | ![]() | 101.7 KB | ||
Masks | ![]() | 244.1 MB | ![]() | |
Filedesc metadata | ![]() | 6.7 KB | ||
Others | ![]() ![]() | 191.3 MB 191.2 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 1 MB | Display | ![]() |
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Full document | ![]() | 1 MB | Display | |
Data in XML | ![]() | 21.7 KB | Display | |
Data in CIF | ![]() | 28.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9jlfMC ![]() 9kmgC ![]() 9kmhC M: atomic model generated by this map C: citing same article ( |
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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: 1.2888 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
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Density Histograms |
-Half map: #2
File | emd_61588_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Escherichia phage FCWL1
Entire | Name: ![]() |
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Components |
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-Supramolecule #1: Escherichia phage FCWL1
Supramolecule | Name: Escherichia phage FCWL1 / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / NCBI-ID: 3136680 / Sci species name: Escherichia phage FCWL1 / Virus type: VIRION / Virus isolate: STRAIN / Virus enveloped: No / Virus empty: No |
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Host (natural) | Organism: ![]() ![]() |
-Macromolecule #1: Terminator protein
Macromolecule | Name: Terminator protein / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 15.191521 KDa |
Sequence | String: MHYELSAAAR AAFLSKYRDF PHYMENRNFT PPKDGGMWLR FNYIEGDTLY LSIDRKCKSY IAIVQIGVVF PPGSGVDEAR LKAKEIADF FKDGKMLNVG YIFEGAIVHQ IVKHESGWMI PVRFTVRVDT KET UniProtKB: Terminator protein |
-Macromolecule #2: Tail tube protein
Macromolecule | Name: Tail tube protein / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 24.21718 KDa |
Sequence | String: MHLPNGAQIF VETSRGEEIE ATAVTNEKNP VATVASKGDL AKGDYVIVTQ STWAKMVSRV LIVTDAQETS ITLAGIDTSD TLVFPAGGT MSFAKITGWT EIPCVQEIGQ DGGEQQYYTY QCLSDDKEQQ IPTFKSAISL TYTFAHEFDN PIYQILRKLD S SGQVTAVR ...String: MHLPNGAQIF VETSRGEEIE ATAVTNEKNP VATVASKGDL AKGDYVIVTQ STWAKMVSRV LIVTDAQETS ITLAGIDTSD TLVFPAGGT MSFAKITGWT EIPCVQEIGQ DGGEQQYYTY QCLSDDKEQQ IPTFKSAISL TYTFAHEFDN PIYQILRKLD S SGQVTAVR MYVPKASEMR MWAGILSFND IPSTQVNEME TVELAVSLKG DFTFISSTLA SPGA UniProtKB: Tail tube protein |
-Macromolecule #3: Portal protein
Macromolecule | Name: Portal protein / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 49.969102 KDa |
Sequence | String: MRYNQGCQLT AFFIGGNMKI VKHDGYNDIF NGGADGSPKP FFMSDASYHV GSFYNDNATA KRIVDVIPEE MVTAGFKISG VKDEKEFKS LWDSYKIDPS LVDALCWARL YGGAAIVAII NDNRMLTSPV KPGAKLEGVR VYDRFAITIE KRVTNARSPR Y GEPEIYKV ...String: MRYNQGCQLT AFFIGGNMKI VKHDGYNDIF NGGADGSPKP FFMSDASYHV GSFYNDNATA KRIVDVIPEE MVTAGFKISG VKDEKEFKS LWDSYKIDPS LVDALCWARL YGGAAIVAII NDNRMLTSPV KPGAKLEGVR VYDRFAITIE KRVTNARSPR Y GEPEIYKV SPGDNIQPYL IHHTRIFIAD GERVTPQMRK QNQGWGASVL NKSLIDAICD YDYCESLATQ ILRRKQQAVW KV KGLAEMC DDDDAQYAAR LRLAQVDDNS GVGRAIGIDA ETEEYDVLNS DISGVPEFLS SKMDRIVSLS GIHEIIIKNK NVG GVSASQ NTALETFYKL VDRKREEDYR PLLEFLLPFI VDEQEWSIEF EPLSVPSKKE ESEITKNNVE SVTKAITEQI IDLE EARDT LRSIAPEFKL KDGNNINIRE PEEPTEPEPG LGEKLEDEN UniProtKB: Portal protein |
-Macromolecule #4: Adaptor protein
Macromolecule | Name: Adaptor protein / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 15.827354 KDa |
Sequence | String: MGVIMNQETL IAAVEQMRKL VPALRKVPDE TLYAWVEMAE LFVCQKTFKD AYVKAIALYA LHLAFLDGAL KGEDEDLESY SRRVTSFSL SGEFSQTFGE VTKNQSGNMM LSTPWGKMFE QLKARRRGRF ALMTGLRGGC H UniProtKB: Adaptor protein |
-Macromolecule #5: Connector protein
Macromolecule | Name: Connector protein / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 13.831523 KDa |
Sequence | String: MNYSQIERMA RKGVAFFTDP SRPMNLIKQG EYGYDENGFE IPPMEQVIPI SGATRRPNAR EIDGETIRAS DILGIFNNDH EINEGDYIE IDGIRHVVVD ARPVQASLEP VAYRPVLRRV SVGG UniProtKB: Connector protein |
-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 |
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Grid | Model: Quantifoil R2/1 / Material: COPPER / Support film - Material: CARBON / Support film - topology: CONTINUOUS / Pretreatment - Type: GLOW DISCHARGE |
Vitrification | Cryogen name: ETHANE / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
Microscope | TFS KRIOS |
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Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 25.8 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.0 µm / Nominal magnification: 75000 |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |