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- EMDB-62948: The composite cryo-EM structure of the head-to-tail connector and... -
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Open data
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Basic information
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Title | The composite cryo-EM structure of the head-to-tail connector and head-proximal tail components of bacteriophage phiXacJX1 | |||||||||
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![]() | Xanthomonas phage / head-to-tail connector / tail / VIRUS | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.6 Å | |||||||||
![]() | Guo M / Wang A / Zheng Y / Liu C / Shao Q / Fang Q | |||||||||
Funding support | 1 items
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![]() | ![]() Title: Cryo-EM structures of a Xanthomonas phage: Insights into viral architecture and implications for the model phage HK97. Authors: Mingcheng Guo / Aohan Wang / Yaqi Zheng / Chaoying Liu / Qianqian Shao / Yunfei Deng / Lin Li / Yueting Wang / Xiaofang Wang / Yue Shen / Jun Qian / Xiaofeng Zhou / Qianglin Fang / ![]() Abstract: Xanthomonas bacteria are responsible for disease outbreaks in several hundred plant species, causing significant economic losses. Xanthomonas phages have emerged as a promising biocontrol strategy in ...Xanthomonas bacteria are responsible for disease outbreaks in several hundred plant species, causing significant economic losses. Xanthomonas phages have emerged as a promising biocontrol strategy in managing various important plant diseases caused by Xanthomonas bacteria. However, structural information for Xanthomonas phages has remained limited so far. Here, we present high-resolution cryo-electron microscopy (cryo-EM) structures of the Xanthomonas citri phage ΦXacJX1 from siphoviruses. These structures include atomic models for the head, head-to-tail connector and head-proximal portion of the tail. ΦXacJX1's head and head-to-tail connector components show significant protein sequence and structural homology with those of the model siphophage HK97. However, the in-situ structures of head-to-tail connector of phage HK97 remain unavailable. The presented structures of phage ΦXacJX1 enhance our understanding of Xanthomonas phages and the mature virion of phage HK97. They provide a valuable framework for future structural and functional studies on both Xanthomonas phages and phage HK97. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 227.8 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 18.2 KB 18.2 KB | Display Display | ![]() |
Images | ![]() | 56.8 KB | ||
Filedesc metadata | ![]() | 6.3 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 584.2 KB | Display | ![]() |
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Full document | ![]() | 583.8 KB | Display | |
Data in XML | ![]() | 7.5 KB | Display | |
Data in CIF | ![]() | 8.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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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: 1.372 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 : Xanthomonas phage phiXacJX1
Entire | Name: ![]() |
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Components |
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-Supramolecule #1: Xanthomonas phage phiXacJX1
Supramolecule | Name: Xanthomonas phage phiXacJX1 / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / NCBI-ID: 3374911 / Sci species name: Xanthomonas phage phiXacJX1 / Virus type: VIRION / Virus isolate: STRAIN / Virus enveloped: No / Virus empty: No |
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Host (natural) | Organism: ![]() |
-Macromolecule #1: portal protein gp1
Macromolecule | Name: portal protein gp1 / type: protein_or_peptide / ID: 1 Details: This protein corresponds to a novel sequence that is not yet available in UniProt. The current reference for the sequence is GenBank Accession Number: PQ476032.1 Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 46.652449 KDa |
Sequence | String: MSENERPGLL GRVMSAFKPK AADAVTVASF SQRDAGLYIG SRFTSDAGRE VSVQTAMSLD AVQACVKLIS QSIAAMPLYL YKKTPDGRK EAVNHPLYDL LLSAPNSSQT AFEFFECILT AMLLHGNAYV RKLMSNGKIE SLQFMHSSRL TISQDARGAY K YAYRKLDG ...String: MSENERPGLL GRVMSAFKPK AADAVTVASF SQRDAGLYIG SRFTSDAGRE VSVQTAMSLD AVQACVKLIS QSIAAMPLYL YKKTPDGRK EAVNHPLYDL LLSAPNSSQT AFEFFECILT AMLLHGNAYV RKLMSNGKIE SLQFMHSSRL TISQDARGAY K YAYRKLDG TQIDVPSAQV WKIRGYSLDG ENGISAIQYG AQVFGTALAA ERQAGRAFTN GNLQQIYYSV AAFLTPEQRE QF SANVAQS VESGRTPVLE GGIDVKALGL NPADAQLLQS RNYSVESICR FFAVPPSMIG HASAGTTSWG SGIEAQQLAF LGL TLAPWL RRIEQSLSLD LLTPGERRQY FVDYDVTTLL RADSAARSSF YATMVNNGVM TRDECREAEG LPKLGGNASV LTVQ SAMVP LDEITNNTGA DPAAAQGTTS LDRSAQ |
-Macromolecule #2: adaptor protein gp5
Macromolecule | Name: adaptor protein gp5 / type: protein_or_peptide / ID: 2 Details: This protein corresponds to a novel sequence that is not yet available in UniProt. The current reference for the sequence is GenBank Accession Number: PQ476032.1 Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 12.313031 KDa |
Sequence | String: MALTLAMVQR HLQADLIEDD ERSYVMEQLL PAARESAEMF LNRNIYSTSE ELAAAVAAGT AGQYPLVTPR AVEQAILLML GDFYRDREA TGKPVSTSAH NLLYPYRVKV GV |
-Macromolecule #3: stopper protein gp6
Macromolecule | Name: stopper protein gp6 / type: protein_or_peptide / ID: 3 Details: This protein corresponds to a novel sequence that is not yet available in UniProt. The current reference for the sequence is GenBank Accession Number: PQ476032.1 Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 13.217896 KDa |
Sequence | String: MPISAGSLKT RLLAQRRTSG TDDWGAPVQG WSDLGLFSGD VKNDTGLGAI RTAAGSGLPA SIAKYSIKVR SEVIRRWSIN SADRIIGRL PFSTQEMVFS VTGVISDFAD PSMAYILVEA GADEQ |
-Macromolecule #4: terminator protein gp8
Macromolecule | Name: terminator protein gp8 / type: protein_or_peptide / ID: 4 Details: This protein corresponds to a novel sequence that is not yet available in UniProt. The current reference for the sequence is GenBank Accession Number: PQ476032.1 Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 13.10487 KDa |
Sequence | String: MTYGPILKQL LSPYFSGRVF PDAAPDVPGQ DPYVIYQRVG GIPTYFTEGA LADKANARVQ LEVWSTSKQA TYEAMVHIMR SVAAAPAME PLGQPIDDYE PALRIYGSRV DISMYYNLT |
-Macromolecule #5: tube protein gp9
Macromolecule | Name: tube protein gp9 / type: protein_or_peptide / ID: 5 Details: This protein corresponds to a novel sequence that is not yet available in UniProt. The current reference for the sequence is GenBank Accession Number: PQ476032.1 Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 22.31592 KDa |
Sequence | String: MALTLPKGIV FGFAPITSTT SSVTGVTRAA PPVATGTMLT AGTTVLVRSN TWTGINNRIS VVDANKALQG FDTTDTTTYP GTSGPVELI TVGAFVNFTQ QGEPSTSGGD QQFWNGQLLE DRSGRQLAIP TFKNAKTLTL PLYMDTSLPW YAAAKAADAR G EPVAVRML ...String: MALTLPKGIV FGFAPITSTT SSVTGVTRAA PPVATGTMLT AGTTVLVRSN TWTGINNRIS VVDANKALQG FDTTDTTTYP GTSGPVELI TVGAFVNFTQ QGEPSTSGGD QQFWNGQLLE DRSGRQLAIP TFKNAKTLTL PLYMDTSLPW YAAAKAADAR G EPVAVRML LPNGDASYNY GYMSFDGDAT ITANAPITNV ATFTFLSDST LVEA |
-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: 7.5 |
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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: 26.0 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: 59000 |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |