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Open data
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Basic information
Entry | ![]() | ||||||||||||
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Title | Cryo-EM structure of bacteriophage T1 tail tip complex | ||||||||||||
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![]() | tail tip complex / VIRAL PROTEIN | ||||||||||||
Function / homology | ![]() symbiont genome ejection through host cell envelope, long flexible tail mechanism / viral tail assembly / virus tail / iron-sulfur cluster binding / host cell cytoplasm / symbiont entry into host cell / membrane Similarity search - Function | ||||||||||||
Biological species | ![]() | ||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 4.3 Å | ||||||||||||
![]() | Chen Y / Liu HR | ||||||||||||
Funding support | ![]()
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![]() | ![]() Title: The In Situ Structure of T-Series T1 Reveals a Conserved Lambda-Like Tail Tip. Authors: Yuan Chen / Hao Xiao / Junquan Zhou / Zeng Peng / Yuning Peng / Jingdong Song / Jing Zheng / Hongrong Liu / ![]() Abstract: It is estimated that over 60% of known tailed phages are siphophages, which are characterized by a long, flexible, and non-contractile tail. Nevertheless, entire high-resolution structures of ...It is estimated that over 60% of known tailed phages are siphophages, which are characterized by a long, flexible, and non-contractile tail. Nevertheless, entire high-resolution structures of siphophages remain scarce. Using cryo-EM, we resolved the structures of T-series siphophage T1, encompassing its head, connector complex, tail tube, and tail tip, at near-atomic resolution. The density maps enabled us to build the atomic models for the majority of T1 proteins. The T1 head comprises 415 copies of the major capsid protein gp47, arranged into an icosahedron with a triangulation number of seven, decorated with 80 homologous trimers and 60 heterotrimers along the threefold and quasi-threefold axes of the icosahedron. The T1 connector complex is composed of two dodecamers (a portal and an adaptor) and two hexamers (a stopper and a tail terminator). The flexible tail tube comprises approximately 34 hexameric rings of tail tube. The extensive disulfide bond network along the successive tail rings may mediate the flexible bending. The distal tip of T1, which is cone-shaped and assembled by proteins gp33, gp34, gp36, gp37, and gp38, displays structural similarity to that of phage lambda. In conjunction with previous studies of lambda-like siphophages, our structure will facilitate further exploration of the structural and mechanistic aspects of lambda-like siphophages. | ||||||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 48.9 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 22.2 KB 22.2 KB | Display Display | ![]() |
Images | ![]() | 56.2 KB | ||
Filedesc metadata | ![]() | 7.3 KB | ||
Others | ![]() ![]() | 48.9 MB 48.9 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 991.7 KB | Display | ![]() |
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Full document | ![]() | 991.3 KB | Display | |
Data in XML | ![]() | 11.7 KB | Display | |
Data in CIF | ![]() | 13.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9l9pMC ![]() 9kzjC ![]() 9l01C ![]() 9l0eC ![]() 9l0fC 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: 1.36 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_62912_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_62912_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Escherichia phage T1
Entire | Name: ![]() |
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Components |
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-Supramolecule #1: Escherichia phage T1
Supramolecule | Name: Escherichia phage T1 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#5 |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: Putative tail fiber protein
Macromolecule | Name: Putative tail fiber protein / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 130.265047 KDa |
Sequence | String: MIQKVISGSK GGSQKPHNPV EMEDNLISIN KIKILLAVSD GEIDETFSLK QLMFNSVPVQ NEDGSFNFEG VKAEFRPGTQ TQEYIKGME DSSSEVTVNR EVTTDNPYTI SVTNKTLSAI RIKMFMPRGV RIESNGDKNG VRVEYEVQQA VDGGSFETVL T DVIEGKTM ...String: MIQKVISGSK GGSQKPHNPV EMEDNLISIN KIKILLAVSD GEIDETFSLK QLMFNSVPVQ NEDGSFNFEG VKAEFRPGTQ TQEYIKGME DSSSEVTVNR EVTTDNPYTI SVTNKTLSAI RIKMFMPRGV RIESNGDKNG VRVEYEVQQA VDGGSFETVL T DVIEGKTM SGYDRSRRVN LPNFNNQVIF RVVRKTPDSN DSNVVDAIQV KSYAEVIDAK FRYPLTGLLF VEFDSKMFPN QL PTISIRK RWKIVNVPSN YDPESRTYNG NWDGTFKKAW TNNPAWVLYD LMINQRYGLD QKELGIAVDK WALYEAAQYC DQM VPDGKG GTEPRYLCDV IIQSQTDAYK VIRDICSIFR GMSFWNGESI SVIIDRPREP AYIFTNDNVV NGDFSYTFAS EKSM YTTCN VMFDDEQNMY QQDVEPVFDR EATLRFGNNV TSITAIGCTR RSEANRRGRW ILKTNLRSTT VNFATGLEGM IPTIG DVVA IADNFWSSNL TMNLSGRLLE VSGSQIFLPF RVDARAGDFI IVNKPDGKPV KRTISSVSAD GKTIEVNIGF GFPVKP NTV FAIDRTDIAL QQYVVTKIDK GDDDEEFTYK ITAVEYDPNK YDEIDYGVNI DDRPTSIVEP DQIPRPKNVQ VSSESRI VQ GMSVETMIVS WDKVPYAVFY DVQWRKDNGN WQNVPQTANK EVYVEGIYAG NYQVRVRSVA GSGTTSGWSN IVAATLTG K QGEPGRPINL TATDDVVFGI RTKWGFSDGS GDTAYTELQQ SPDGTVDNAS LLSLIPYPQH EYYHSPMPGG NIVWYRVRT VDRIGNVSQW TDFVRGMAST NVDDIIGEIS VDIENSPGYE WLVDNATDNA AQNSANAEAA IENALANDKD AIYMKKENGK RKAEYTKSL KLIADETQAR VTAIEQLKAS FGDQISASNS ELREVIATET EALSREIDQL KAQIGDDIQA SLTDIREVIA T ETEALSRE IDQLKAQIGD DIQASLTDIR EAIANETEAR TQADLTLSAR LGNNEAALAQ KLDSWSNADS TGAMYGVKLG LK YNGQEYS AGMAMSLVGS GAAVKAQILF EASRFAIMTG MNGQTQYPFV VENGQVILSS AIIKNGFITN AMIGNFIQSN NYV FNQSGW RLDKGGTFEN YGSDGEGAMK QTNTTISVRD ASGRLRVQIG RLTGSW UniProtKB: Putative tail fiber protein |
-Macromolecule #2: Putative tail assembly protein
Macromolecule | Name: Putative tail assembly protein / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 20.916922 KDa |
Sequence | String: MNDVKVIKLS GSLGRRFGVF HRYAVDSYPE AIRALSSQVD GFKEYMQSEV GSRSKFAIFV DGVNVGHHEE EKFKCAKEIR IVPIPTGSK TGGLFQVVLG AAIMVAAFYT GGASLALMGT MSSSLFMMGG AMVLGGVMQM ISPQPGGANF EVQSSKNKPS Y AFGGAVNT ...String: MNDVKVIKLS GSLGRRFGVF HRYAVDSYPE AIRALSSQVD GFKEYMQSEV GSRSKFAIFV DGVNVGHHEE EKFKCAKEIR IVPIPTGSK TGGLFQVVLG AAIMVAAFYT GGASLALMGT MSSSLFMMGG AMVLGGVMQM ISPQPGGANF EVQSSKNKPS Y AFGGAVNT TAAGYPLPVP YGYRAGGGAT FSAGSYAEDM S UniProtKB: Putative tail assembly protein |
-Macromolecule #3: Putative minor tail protein
Macromolecule | Name: Putative minor tail protein / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 29.058648 KDa |
Sequence | String: MSENKKLYDE ESGKSLFHNC LQSLYPGEII TLIEVDGSKF GAQVYRFHGE NIQYTPEEIM QAQQTGTLPP KEITFRGEKY GARPFGISG ISFDSSGKAT KPQLTVANID SRVSAMIRAY NGLMQAKVTI WITQRELINS DGSIADGAYR KLVYYIERPN Y VDKSVARF ...String: MSENKKLYDE ESGKSLFHNC LQSLYPGEII TLIEVDGSKF GAQVYRFHGE NIQYTPEEIM QAQQTGTLPP KEITFRGEKY GARPFGISG ISFDSSGKAT KPQLTVANID SRVSAMIRAY NGLMQAKVTI WITQRELINS DGSIADGAYR KLVYYIERPN Y VDKSVARF DLTSPYDMDG IMIPSRLTQS VCYFAQRGWY KTGKGCGYNG QNGYFDKDNN PVDDPSLDFC PGTVTACRLR FG ANNELDF GGCAVASLQR KNQ UniProtKB: Putative minor tail protein |
-Macromolecule #4: Putative minor tail protein
Macromolecule | Name: Putative minor tail protein / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 12.992562 KDa |
Sequence | String: MATLDTFGWC TQVQGGGGSL TTTNSDRSIQ FGNGYMQLAS SGFNTTRREY SVVYAGEDFM AVYDFCNSHR IKPFAWTPPD GKIGIWVVK PNSLGAKPVS RDVMEINVTF MEQFTSME UniProtKB: Putative minor tail protein |
-Macromolecule #5: Tape measure protein
Macromolecule | Name: Tape measure protein / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 103.784391 KDa |
Sequence | String: MVDKVAGLSL DVDVSTVQRA VKSLKEFSKA NDQAADSMGS LINESEVAKQ KAKEHAEQLR RQRKEYEAVE KAIDPTVSKM ERLKIASQQ LDKLWQQGVV PDETFFRLGE MLDLQNAKLA RSRAMLTEEG QAALQEAKAK EQAAVRSKAF MDALNGQVNA I GKTHAELM ...String: MVDKVAGLSL DVDVSTVQRA VKSLKEFSKA NDQAADSMGS LINESEVAKQ KAKEHAEQLR RQRKEYEAVE KAIDPTVSKM ERLKIASQQ LDKLWQQGVV PDETFFRLGE MLDLQNAKLA RSRAMLTEEG QAALQEAKAK EQAAVRSKAF MDALNGQVNA I GKTHAELM ELKAAELGLS KEAAPLIAKL KDQGRAMNAA GISAGEYRQA MRMLPAQITD VVTSLASGMP VWMVAIQQGG QI KDSFGGI GNTFKVLLSY INPVTAGVGV LVGSLGILAK AGYDSYKSIT DIQNALIETG GYAGVTAEEL DSVSKKIAQT SNS TIGSIR EIVTELASSG KYTREQIQNI TKATAEWSAS TGKSASQIIS EFEKIASDPV KGLKKLNEQY NFLEKGQLTY IDTL SRTKG ETEAVSEATK LFADVMEKRM KSIADNATPL EKMWSDIKQW ASDAWGWVGD HTLGALNLII DVVQGTVIQV KMILA KGDE YISNFIASAI KATQSLPGMS DFGADVLKEQ ENIVKSSRDN YDQLASDLDA INARVEKGEM GYIEAMRQRR TLEKQY SEE TKEAIRKEAE EIEKRNRERN KQSKIVRSPT EQFDKELISL RAQLKVLQEH KEIGQKLSAQ RKALFTTEAT IAVLREA SS KRQLSAEEKA LLASQERVIE LAKQKAEIGD QIVKQQQLND LTDKSLKFVN EMTAATEQLN ASRGLSTRDM ERQAELAK I TTDYINSGGS EGDEKLQNMI KAQNDYYAAE DAKRADWLAG AESAFADYGD AAMDMYGNVN EIASSALNGM SDMMVQFLT TGKANFEDFA KNIIGMIIKM IAQMVIFNTI SGMMGGKTWS FAGGASSGAS AASQATPTPA ASVFRSVSSG GAAVSLAAAA GSVATSGFN ASNSAPKVVN HSGGGTVVDV SGMEVKVDNG SDPRGISQGV EMMFKKMIRE SCSQGGEVYN YIQEKTGG UniProtKB: Tape measure protein |
-Macromolecule #6: IRON/SULFUR CLUSTER
Macromolecule | Name: IRON/SULFUR CLUSTER / type: ligand / ID: 6 / Number of copies: 1 / Formula: SF4 |
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Molecular weight | Theoretical: 351.64 Da |
Chemical component information | ![]() ChemComp-FS1: |
-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: 7.6 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | TFS KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 32.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 4.0 µm / Nominal defocus min: 2.0 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |