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PDBsum entry 6j0c

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protein Protein-protein interface(s) links
Protein transport PDB id
6j0c

 

 

 

 

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Contents
Protein chains
(+ 6 more) 354 a.a.
PDB id:
6j0c
Name: Protein transport
Title: Cryo-em structure of an extracellular contractile injection system, pvc sheath complex in contracted state
Structure: Pvc2. Chain: a, b, c, d, e, f, a, b, c, d, e, f. Engineered: yes
Source: Photorhabdus asymbiotica subsp. Asymbiotica (strain atcc 43949 / 3105-77). Xenorhabdus luminescens (strain 2). Organism_taxid: 553480. Strain: atcc 43949 / 3105-77. Gene: pau_03352, pa-rva20-21-0170. Expressed in: escherichia coli. Expression_system_taxid: 562
Authors: F.Jiang,N.Li,X.Wang,J.Cheng,Y.Huang,Y.Yang,J.Yang,B.Cai,Y.Wang,Q.Jin, N.Gao
Key ref: F.Jiang et al. (2019). Cryo-EM Structure and Assembly of an Extracellular Contractile Injection System. Cell, 177, 370. PubMed id: 30905475 DOI: 10.1016/j.cell.2019.02.020
Date:
23-Dec-18     Release date:   10-Apr-19    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
B6VNP3  (B6VNP3_PHOAA) -  Phage tail sheath protein from Photorhabdus asymbiotica subsp. asymbiotica (strain ATCC 43949 / 3105-77)
Seq:
Struc:
355 a.a.
354 a.a.
Key:    PfamA domain  Secondary structure

 Enzyme reactions 
   Enzyme class: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
DOI no: 10.1016/j.cell.2019.02.020 Cell 177:370 (2019)
PubMed id: 30905475  
 
 
Cryo-EM Structure and Assembly of an Extracellular Contractile Injection System.
F.Jiang, N.Li, X.Wang, J.Cheng, Y.Huang, Y.Yang, J.Yang, B.Cai, Y.P.Wang, Q.Jin, N.Gao.
 
  ABSTRACT  
 
Contractile injection systems (CISs) are cell-puncturing nanodevices that share ancestry with contractile tail bacteriophages. Photorhabdus virulence cassette (PVC) represents one group of extracellular CISs that are present in both bacteria and archaea. Here, we report the cryo-EM structure of an intact PVC from P. asymbiotica. This over 10-MDa device resembles a simplified T4 phage tail, containing a hexagonal baseplate complex with six fibers and a capped 117-nanometer sheath-tube trunk. One distinct feature of the PVC is the presence of three variants for both tube and sheath proteins, indicating a functional specialization of them during evolution. The terminal hexameric cap docks onto the topmost layer of the inner tube and locks the outer sheath in pre-contraction state with six stretching arms. Our results on the PVC provide a framework for understanding the general mechanism of widespread CISs and pave the way for using them as delivery tools in biological or therapeutic applications.
 

 

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