5OES

The structure of a glutathione synthetase (StGSS1) from Solanum tuberosum in ADP and y-EC bound closed conformation.


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.48 Å
  • R-Value Free: 0.241 
  • R-Value Work: 0.224 
  • R-Value Observed: 0.225 

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Literature

Effector gene birth in plant parasitic nematodes: Neofunctionalization of a housekeeping glutathione synthetase gene.

Lilley, C.J.Maqbool, A.Wu, D.Yusup, H.B.Jones, L.M.Birch, P.R.J.Banfield, M.J.Urwin, P.E.Eves-van den Akker, S.

(2018) PLoS Genet 14: e1007310-e1007310

  • DOI: https://doi.org/10.1371/journal.pgen.1007310
  • Primary Citation of Related Structures:  
    5OES, 5OET, 5OEU, 5OEV

  • PubMed Abstract: 

    Plant pathogens and parasites are a major threat to global food security. Plant parasitism has arisen four times independently within the phylum Nematoda, resulting in at least one parasite of every major food crop in the world. Some species within the most economically important order (Tylenchida) secrete proteins termed effectors into their host during infection to re-programme host development and immunity. The precise detail of how nematodes evolve new effectors is not clear. Here we reconstruct the evolutionary history of a novel effector gene family. We show that during the evolution of plant parasitism in the Tylenchida, the housekeeping glutathione synthetase (GS) gene was extensively replicated. New GS paralogues acquired multiple dorsal gland promoter elements, altered spatial expression to the secretory dorsal gland, altered temporal expression to primarily parasitic stages, and gained a signal peptide for secretion. The gene products are delivered into the host plant cell during infection, giving rise to "GS-like effectors". Remarkably, by solving the structure of GS-like effectors we show that during this process they have also diversified in biochemical activity, and likely represent the founding members of a novel class of GS-like enzyme. Our results demonstrate the re-purposing of an endogenous housekeeping gene to form a family of effectors with modified functions. We anticipate that our discovery will be a blueprint to understand the evolution of other plant-parasitic nematode effectors, and the foundation to uncover a novel enzymatic function.


  • Organizational Affiliation

    Centre for Plant Sciences, Faculty of Biological Sciences, University of Leeds, Leeds, United Kingdom.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Glutathione synthetase
A, B, C, D, E
A, B, C, D, E, F
483Solanum tuberosumMutation(s): 0 
EC: 6.3.2.3
UniProt
Find proteins for M1CSC4 (Solanum tuberosum)
Explore M1CSC4 
Go to UniProtKB:  M1CSC4
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupM1CSC4
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 3 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
ADP
Query on ADP

Download Ideal Coordinates CCD File 
G [auth A]
K [auth B]
N [auth C]
R [auth D]
V [auth E]
G [auth A],
K [auth B],
N [auth C],
R [auth D],
V [auth E],
Z [auth F]
ADENOSINE-5'-DIPHOSPHATE
C10 H15 N5 O10 P2
XTWYTFMLZFPYCI-KQYNXXCUSA-N
3GC
Query on 3GC

Download Ideal Coordinates CCD File 
AA [auth F]
H [auth A]
L [auth B]
O [auth C]
S [auth D]
AA [auth F],
H [auth A],
L [auth B],
O [auth C],
S [auth D],
W [auth E]
GAMMA-GLUTAMYLCYSTEINE
C8 H14 N2 O5 S
RITKHVBHSGLULN-WHFBIAKZSA-N
MG
Query on MG

Download Ideal Coordinates CCD File 
BA [auth F]
I [auth A]
J [auth A]
M [auth B]
P [auth C]
BA [auth F],
I [auth A],
J [auth A],
M [auth B],
P [auth C],
Q [auth C],
T [auth D],
U [auth D],
X [auth E],
Y [auth E]
MAGNESIUM ION
Mg
JLVVSXFLKOJNIY-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.48 Å
  • R-Value Free: 0.241 
  • R-Value Work: 0.224 
  • R-Value Observed: 0.225 
  • Space Group: P 41 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 154.39α = 90
b = 154.39β = 90
c = 344.325γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
PDB_EXTRACTdata extraction
xia2data reduction
xia2data processing
MOLREPphasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Biotechnology and Biological Sciences Research CouncilUnited KingdomBB/M014207/1

Revision History  (Full details and data files)

  • Version 1.0: 2018-04-25
    Type: Initial release
  • Version 1.1: 2024-01-17
    Changes: Data collection, Database references, Derived calculations, Refinement description