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Open data
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Basic information
Entry | ![]() | |||||||||||||||
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Title | Shigella flexneri bacteriophage Moo19 Tail | |||||||||||||||
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![]() | Moo19 / VIRUS | |||||||||||||||
Function / homology | ![]() : / Phage SU10 portal protein / Tail spike TSP1/Gp66, N-terminal domain / Tail spike TSP1/Gp66 receptor binding N-terminal domain / SGNH hydrolase-type esterase domain / GDSL-like Lipase/Acylhydrolase family / SGNH hydrolase superfamily Similarity search - Domain/homology | |||||||||||||||
Biological species | ![]() | |||||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.7 Å | |||||||||||||||
![]() | Subramanian S / Bergland Drarvik SM / Parent KN | |||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Moo19 and B2: Structures of podophages with = 9 geometry and tailspikes with esterase activity. Authors: Sundharraman Subramanian / Silje M Bergland Drarvik / Kendal R Tinney / Sarah M Doore / Kristin N Parent / ![]() Abstract: Podophages are, by far, the least well studied of all the bacteriophages. Despite being classified together due to their short, noncontractile tails, there is a huge amount of diversity among members ...Podophages are, by far, the least well studied of all the bacteriophages. Despite being classified together due to their short, noncontractile tails, there is a huge amount of diversity among members of this group. Of the podophages, the N4-like family is the least well studied structurally and is quite divergent from well-characterized podophages such as T7 and P22. In this work, we isolate and fully characterize two members of the family by cryo-electron microscopy, genetics, and biochemistry. We describe the capsid features of Moo19 and B2, including a decoration protein. In addition, we have fully modeled the tail machinery for both phages and identify proteins with esterase activity. Genetic knockouts of the host reveal factors specific for host attachment including key modifications to the O-antigen on the lipopolysaccharide. Moo19 and B2 are both members, yet some distinct differences in the genome and structure place them into distinct clades. | |||||||||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 39.5 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 21 KB 21 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 17.6 KB | Display | ![]() |
Images | ![]() | 203.6 KB | ||
Masks | ![]() | 476.8 MB | ![]() | |
Filedesc metadata | ![]() | 7 KB | ||
Others | ![]() ![]() | 371.5 MB 371.5 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 729.3 KB | Display | ![]() |
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Full document | ![]() | 728.8 KB | Display | |
Data in XML | ![]() | 25.4 KB | Display | |
Data in CIF | ![]() | 34.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9d80MC ![]() 9d7zC ![]() 9d81C ![]() 9d82C ![]() 9d83C ![]() 9d84C 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: 1.632 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: #1
File | emd_46623_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_46623_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Shigella virus Moo19
Entire | Name: ![]() |
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Components |
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-Supramolecule #1: Shigella virus Moo19
Supramolecule | Name: Shigella virus Moo19 / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / NCBI-ID: 2886042 / Sci species name: Shigella virus Moo19 / Virus type: VIRION / Virus isolate: OTHER / Virus enveloped: No / Virus empty: No |
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Host (natural) | Organism: ![]() |
-Macromolecule #1: Portal protein
Macromolecule | Name: Portal protein / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 85.342766 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MEHQDSMTPL PDPGQSDKLT NWKKEPSIQT LKADLEAGKP AHDAIMKEIQ KWNDLMKAEG SAKPPKVKGR SQVQPKLVRR QAEWRYAPL SEPFLSSPKL FKLTPVTWED EQAARQNELV LNYQFRTQLN RVKLVDDYVH SVCDDGTGIA RVGWERKVVK V KQDAPVFQ ...String: MEHQDSMTPL PDPGQSDKLT NWKKEPSIQT LKADLEAGKP AHDAIMKEIQ KWNDLMKAEG SAKPPKVKGR SQVQPKLVRR QAEWRYAPL SEPFLSSPKL FKLTPVTWED EQAARQNELV LNYQFRTQLN RVKLVDDYVH SVCDDGTGIA RVGWERKVVK V KQDAPVFQ MYPVETEEQV QILQQALDLQ AQNPRGYEEQ VADDVKEAVN YFNETGEATY AIQTGTTEVE VEKAVVNRPT VE MLDPNNV VIDPSCNGDL DRALFAVVSF ETCKADLLKT PDRYHNLDKI DWESSSPLTD PDHESKTPGD FQFRDAMRKR VIA YEYWGF WDTNGDGELK PIVATWIGTT LIRMEENPYP DGKLPFVLVP YMPRKRELYG EADAELLGDN QKILGATMRG MIDL LGRSA NGQRAYPKGM LDTLNRRRFE DGLDYEYNPQ TGNPSQAIIE HKFPELPQSA IVMSQMQNQE AEALTGVKAF AGGVT GSAY GDVAAGIRGA LDAASKREMA ILRRLAKGMA DIGTKICAMN AVFLSETEVV RITNEEYVTI NREDLKGNFD IEVDIN TAE VDNQKSQDLG FMVQTIGNTV DQQVTLKLVA RIAELKRMPE LAHELRTWKP EPDPMEEQLK QLAIQKAQLE NQKLQSE IA LNEAKVRAED AKKDMTNLDY LEQESGTKHA REMEKQKAQS QGNQNLQVTK ALTQPVKEGE TSPNISAAIG YNAITDGN N QVNNELERDA LAPQDPSLSI GSQYFDPSRD PALSPGMNL UniProtKB: Portal protein |
-Macromolecule #2: Gp83
Macromolecule | Name: Gp83 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 26.990467 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MRKLSDVYKV LALTSLKSAG FITDDKVNIE AWGKPEVLAH INEGLTRLHS RFVLRTNNCI VEMKEGRTDY PLLARYSYER FDPAKAPYP YIMDTPQEPF QEDVIKILNV YDSKGIRRKL NDDHDKNGLF TPRPDVLQCM WPRHFEALNV LYQAKHPELT G DENQEIDL ...String: MRKLSDVYKV LALTSLKSAG FITDDKVNIE AWGKPEVLAH INEGLTRLHS RFVLRTNNCI VEMKEGRTDY PLLARYSYER FDPAKAPYP YIMDTPQEPF QEDVIKILNV YDSKGIRRKL NDDHDKNGLF TPRPDVLQCM WPRHFEALNV LYQAKHPELT G DENQEIDL PETLYSALEN WVGYRYHTGL NTEGSTAKAA EYLQLYESIC GEVVDFDLAN GSMSNTNVLF EKRGWV UniProtKB: Uncharacterized protein |
-Macromolecule #3: Tail protein
Macromolecule | Name: Tail protein / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 30.295928 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MSCGAEVEAN RLLLALTEGE DFALPDIDMS GPEWDIPGGD GSPIFAEVTR LTNEDLTTRV VGGSGTFDAL MASAAAHLKQ EFKEGRITG GEYTKAYIAI VETCMGNATQ YLLGRDQAYW AAAMAQIQAV SARVALATSK AQYVLAKFQA LNAKSEYALT K LKLSTESE ...String: MSCGAEVEAN RLLLALTEGE DFALPDIDMS GPEWDIPGGD GSPIFAEVTR LTNEDLTTRV VGGSGTFDAL MASAAAHLKQ EFKEGRITG GEYTKAYIAI VETCMGNATQ YLLGRDQAYW AAAMAQIQAV SARVALATSK AQYVLAKFQA LNAKSEYALT K LKLSTESE TYCAALFNVE QTLPQQLKLL IEQTEAQRAQ TLDKRSDGAT VSGSIGKQKE LYTQQITSYQ RDAEVKASKL FT DAWITQK TIDEGLTPPN GFTNSSIDDV LTTLKRNNNL NG UniProtKB: Tail protein |
-Macromolecule #4: Tail fiber protein
Macromolecule | Name: Tail fiber protein / type: protein_or_peptide / ID: 4 / Number of copies: 3 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 118.004133 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MGMNSHIPFD ADNDWTLDPY HCNRSNDPLV DKVIGNAYAV VRAVYCNLGN LKLLYDFLNT YGMVLGVKSE AELKKLNKLA KYARVYGFA DTGDRQVTDY LYVPDDTSGI RPDDQTATGS WIKVSTSGSG SGGTGGGSGS YIPYVYANGS ALGGETSFKV P AEALGVPF ...String: MGMNSHIPFD ADNDWTLDPY HCNRSNDPLV DKVIGNAYAV VRAVYCNLGN LKLLYDFLNT YGMVLGVKSE AELKKLNKLA KYARVYGFA DTGDRQVTDY LYVPDDTSGI RPDDQTATGS WIKVSTSGSG SGGTGGGSGS YIPYVYANGS ALGGETSFKV P AEALGVPF IIINGSVQYI GYGFSFNPAN STVTLSNPLV QGDEVIALTS AAPASPDNPN VSNWVQVNWL YNNGAAVGGE QV ITVPYNF KDVPAVYKNG ERYYKNLQTK SYVYDPSTRT VTMTELLAQG DRVIITLGGE SASLEITDRT TQEVARANNV KDT DVVLSS STNVVITDKK VLYDVNAQKY WDLPNLPPNV YIVKVEGNKL IYNPGAVVID LLEPANPLVI VEPVLSRLGA ETGN PMAGT FEKGATVDSA AKSVGSTMEG KLYRWEGALP KTVRAGDTPS SSGGIGSGKW VEITNATLRS QLASTGGAAM VKASD GRTV EQWLVQSDSA SFRAKNMAKL AWCDYQVHNR GSLKCCFLGD SMTAGFDRTS SDTIPAQDGD WATRASMNYP YRFASY LPE QSGCSVYITM RAISGYTAKQ AYEEALWQSN PNCDIVFIMY AINDSGGVAG ATLDLYMEYM EKLIRRYIDW GCAVVVQ RP SGGGQGAGNP AWLHWAKRMQ MVARVYGCPV FDAHEVMLNR HYAAVQSDGT HYNSMGYAIH GEKLASMLMA GGLLDTYK P VVNETTVWTG MMSDHIGWCD ARGNIGTGRS DGAYTRDKVT GVLQAGKATI CTFSFYLDAE AAHIYGKLDG LINTIYTNG YWWNNGNKPY YQYAVDIDNS FGASLQRVNK SANNYEGMPG SRKFVGRLIG RGWHTITLFT NLQGEALKDA FVNSITVQPI PIGLSTEQM WGQDEERRYR VVHTRRMPSP SGQGGTLPVA VALTGFQMRA PQSFLGTGPG TNAVPAPYFY NTVPGKLKVY N EKGDYIEW LVYKDGSSGL KWKGKVLTHS FADVASVPTL TAYMGTAKQN VIVAAGSSGA NQPLENIYDY NAGLQEQTGN PS TDLSWKG GIYLVFTLAW PSTAPTGYWT IELEGSDWFG NSESAVGCF UniProtKB: Tail fiber 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: 7.5 Component:
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Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277.15 K / Instrument: FEI VITROBOT MARK IV |
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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: 33.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.5 µm / Nominal defocus min: 0.5 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |