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PDBsum entry 5o2y

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protein metals links
Protein transport PDB id
5o2y

 

 

 

 

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Contents
Protein chain
116 a.a.
Metals
_CA
PDB id:
5o2y
Name: Protein transport
Title: Nmr structure of the calcium bound form of pulg, major pseudopilin from klebsiella oxytoca t2ss
Structure: General secretion pathway protein g. Chain: a. Synonym: general secretion pathway protein gspg. Engineered: yes
Source: Klebsiella oxytoca. Organism_taxid: 571. Gene: pulg, ab185_31145, samea2273639_02747. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008
NMR struc: 15 models
Authors: A.Lopez-Castilla,B.Bardiaux,B.Vitorge,J.-L.Thomassin,W.Zheng,X.Yu, E.H.Egelman,M.Nilges,O.Francetic,N.Izadi-Pruneyre
Key ref: A.López-Castilla et al. (2017). Structure of the calcium-dependent type 2 secretion pseudopilus. Nat Microbiol, 2, 1686-1695. PubMed id: 28993624
Date:
23-May-17     Release date:   18-Oct-17    
PROCHECK
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 Headers
 References

Protein chain
A0A0G3SCW3  () - 
Key:    Secondary structure

 

 
Nat Microbiol 2:1686-1695 (2017)
PubMed id: 28993624  
 
 
Structure of the calcium-dependent type 2 secretion pseudopilus.
A.López-Castilla, J.L.Thomassin, B.Bardiaux, W.Zheng, M.Nivaskumar, X.Yu, M.Nilges, E.H.Egelman, N.Izadi-Pruneyre, O.Francetic.
 
  ABSTRACT  
 
Many Gram-negative bacteria use type 2 secretion systems (T2SSs) to secrete proteins involved in virulence and adaptation. Transport of folded proteins via T2SS nanomachines requires the assembly of inner membrane-anchored fibres called pseudopili. Although efficient pseudopilus assembly is essential for protein secretion, structure-based functional analyses are required to unravel the mechanistic link between these processes. Here, we report an atomic model for a T2SS pseudopilus from Klebsiella oxytoca, obtained by fitting the NMR structure of its calcium-bound subunit PulG into the ~5-Å-resolution cryo-electron microscopy reconstruction of assembled fibres. This structure reveals the comprehensive network of inter-subunit contacts and unexpected features, including a disordered central region of the PulG helical stem, and highly flexible C-terminal residues on the fibre surface. NMR, mutagenesis and functional analyses highlight the key role of calcium in PulG folding and stability. Fibre disassembly in the absence of calcium provides a basis for pseudopilus length control, essential for protein secretion, and supports the Archimedes screw model for the type 2 secretion mechanism.
 

 

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