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PDBsum entry 6u5h

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protein Protein-protein interface(s) links
Unknown function PDB id
6u5h

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
318 a.a.
PDB id:
6u5h
Name: Unknown function
Title: Cryoem structure of pyocin r2 - precontracted - hub
Structure: Probable bacteriophage protein pyocin r2. Chain: c, b, a
Source: Pseudomonas aeruginosa (strain atcc 15692 / dsm 22644 / cip 104116 / jcm 14847 / lmg 12228 / 1c / prs 101 / pao1). Organism_taxid: 208964. Strain: atcc 15692 / dsm 22644 / cip 104116 / jcm 14847 / lmg 12228 / 1c / prs 101 / pao1
Authors: P.Ge,J.Avaylon,D.Scholl,M.M.Shneider,C.Browning,S.A.Buth,M.Plattner, K.Ding,P.G.Leiman,J.F.Miller,Z.H.Zhou
Key ref: P.Ge et al. (2020). Action of a minimal contractile bactericidal nanomachine. Nature, 580, 658-662. PubMed id: 32350467 DOI: 10.1038/s41586-020-2186-z
Date:
27-Aug-19     Release date:   15-Apr-20    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
G3XCU8  (G3XCU8_PSEAE) -  Phage late control D family protein from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Seq:
Struc:
329 a.a.
318 a.a.
Key:    PfamA domain  Secondary structure

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

 

 
DOI no: 10.1038/s41586-020-2186-z Nature 580:658-662 (2020)
PubMed id: 32350467  
 
 
Action of a minimal contractile bactericidal nanomachine.
P.Ge, D.Scholl, N.S.Prokhorov, J.Avaylon, M.M.Shneider, C.Browning, S.A.Buth, M.Plattner, U.Chakraborty, K.Ding, P.G.Leiman, J.F.Miller, Z.H.Zhou.
 
  ABSTRACT  
 
R-type bacteriocins are minimal contractile nanomachines that hold promise as precision antibiotics1-4. Each bactericidal complex uses a collar to bridge a hollow tube with a contractile sheath loaded in a metastable state by a baseplate scaffold1,2. Fine-tuning of such nucleic acid-free protein machines for precision medicine calls for an atomic description of the entire complex and contraction mechanism, which is not available from baseplate structures of the (DNA-containing) T4 bacteriophage5. Here we report the atomic model of the complete R2 pyocin in its pre-contraction and post-contraction states, each containing 384 subunits of 11 unique atomic models of 10 gene products. Comparison of these structures suggests the following sequence of events during pyocin contraction: tail fibres trigger lateral dissociation of baseplate triplexes; the dissociation then initiates a cascade of events leading to sheath contraction; and this contraction converts chemical energy into mechanical force to drive the iron-tipped tube across the bacterial cell surface, killing the bacterium.
 

 

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