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Open data
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Basic information
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Title | SaPI1 portal structure in mature capsids without DNA | |||||||||||||||
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![]() | portal / phage / sapi / STRUCTURAL PROTEIN | |||||||||||||||
Biological species | ![]() | |||||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.5 Å | |||||||||||||||
![]() | Mukherjee A / Kizziah JL / Dokland T | |||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Structure of the Portal Complex from Staphylococcus aureus Pathogenicity Island 1 Transducing Particles In Situ and In Isolation. Authors: Amarshi Mukherjee / James L Kizziah / N'Toia C Hawkins / Mohamed O Nasef / Laura K Parker / Terje Dokland / ![]() Abstract: Staphylococcus aureus is an important human pathogen, and the prevalence of antibiotic resistance is a major public health concern. The evolution of pathogenicity and resistance in S. aureus often ...Staphylococcus aureus is an important human pathogen, and the prevalence of antibiotic resistance is a major public health concern. The evolution of pathogenicity and resistance in S. aureus often involves acquisition of mobile genetic elements (MGEs). Bacteriophages play an especially important role, since transduction represents the main mechanism for horizontal gene transfer. S. aureus pathogenicity islands (SaPIs), including SaPI1, are MGEs that carry genes encoding virulence factors, and are mobilized at high frequency through interactions with specific "helper" bacteriophages, such as 80α, leading to packaging of the SaPI genomes into virions made from structural proteins supplied by the helper. Among these structural proteins is the portal protein, which forms a ring-like portal at a fivefold vertex of the capsid, through which the DNA is packaged during virion assembly and ejected upon infection of the host. We have used high-resolution cryo-electron microscopy to determine structures of the S. aureus bacteriophage 80α portal itself, produced by overexpression, and in situ in the empty and full SaPI1 virions, and show how the portal interacts with the capsid. These structures provide a basis for understanding portal and capsid assembly and the conformational changes that occur upon DNA packaging and ejection. | |||||||||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 158.4 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 16.5 KB 16.5 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 12.7 KB | Display | ![]() |
Images | ![]() | 161.2 KB | ||
Masks | ![]() | 178 MB | ![]() | |
Filedesc metadata | ![]() | 5.8 KB | ||
Others | ![]() ![]() | 136.4 MB 136 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 1.1 MB | Display | ![]() |
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Full document | ![]() | 1.1 MB | Display | |
Data in XML | ![]() | 20.1 KB | Display | |
Data in CIF | ![]() | 26.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8vdcMC ![]() 8v8bC ![]() 8vd4C ![]() 8vd5C ![]() 8vd8C ![]() 8vdeC C: citing same article ( M: atomic model generated by this map |
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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: 1.33 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
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Density Histograms |
-Half map: #1
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Density Histograms |
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Sample components
-Entire : Dubowvirus dv80alpha
Entire | Name: ![]() |
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Components |
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-Supramolecule #1: Dubowvirus dv80alpha
Supramolecule | Name: Dubowvirus dv80alpha / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / NCBI-ID: 53369 / Sci species name: Dubowvirus dv80alpha / Virus type: SATELLITE / Virus isolate: SPECIES / Virus enveloped: No / Virus empty: No |
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-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: 59.55182 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MLKVNEFETD TDLRGNINYL FNDEANVVYT YDGTESDLLQ NVNEVSKYIE HHMDYQRPRL KVLSDYYEGK TKNLVELTRR KEEYMADNR VAHDYASYIS DFINGYFLGN PIQYQDDDKD VLEAIEAFND LNDVESHNRS LGLDLSIYGK AYELMIRNQD D ETRLYKSD ...String: MLKVNEFETD TDLRGNINYL FNDEANVVYT YDGTESDLLQ NVNEVSKYIE HHMDYQRPRL KVLSDYYEGK TKNLVELTRR KEEYMADNR VAHDYASYIS DFINGYFLGN PIQYQDDDKD VLEAIEAFND LNDVESHNRS LGLDLSIYGK AYELMIRNQD D ETRLYKSD AMSTFIIYDN TVERNSIAGV RYLRTKPIDK TDEDEVFTVD LFTSHGVYRY LTNRTNGLKL TPRENSFESH SF ERMPITE FSNNERRKGD YEKVITLIDL YDNAESDTAN YMSDLNDAML LIKGNLNLDP VEVRKQKEAN VLFLEPTVYV DAE GRETEG SVDGGYIYKQ YDVQGTEAYK DRLNSDIHMF TNTPNMKDDN FSGTQSGEAM KYKLFGLEQR TKTKEGLFTK GLRR RAKLL ETILKNTRSI DANKDFNTVR YVYNRNLPKS LIEELKAYID SGGKISQTTL MSLFSFFQDP ELEVKKIEED EKESI KKAQ KGIYKDPRDI NDDEQDDDTK DTVDKKE |
-Macromolecule #2: Connector
Macromolecule | Name: Connector / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 12.809583 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MTTLADVKKR IGLKDEKQDE QLEEIIKSCE SQLLSMLPIE VEQIPERFSY MIKEVAVKRY NRIGAEGMTS EAVDGRSNAY ELNDFKEYE AIIDNYFNAR TRTKKGRAVF F |
-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: 7.8 |
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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: 35.26 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.7000000000000001 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |