4LVN

Crystal structure of PfSUB1-prodomain-NIMP.M7 Fab complex


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.25 Å
  • R-Value Free: 0.237 
  • R-Value Work: 0.195 
  • R-Value Observed: 0.198 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

The malaria parasite egress protease SUB1 is a calcium-dependent redox switch subtilisin.

Withers-Martinez, C.Strath, M.Hackett, F.Haire, L.F.Howell, S.A.Walker, P.A.Evangelos, C.Dodson, G.G.Blackman, M.J.

(2014) Nat Commun 5: 3726-3726

  • DOI: https://doi.org/10.1038/ncomms4726
  • Primary Citation of Related Structures:  
    4LVN, 4LVO

  • PubMed Abstract: 

    Malaria is caused by a protozoan parasite that replicates within an intraerythrocytic parasitophorous vacuole. Release (egress) of malaria merozoites from the host erythrocyte is a highly regulated and calcium-dependent event that is critical for disease progression. Minutes before egress, an essential parasite serine protease called SUB1 is discharged into the parasitophorous vacuole, where it proteolytically processes a subset of parasite proteins that play indispensable roles in egress and invasion. Here we report the first crystallographic structure of Plasmodium falciparum SUB1 at 2.25 Å, in complex with its cognate prodomain. The structure highlights the basis of the calcium dependence of SUB1, as well as its unusual requirement for interactions with substrate residues on both prime and non-prime sides of the scissile bond. Importantly, the structure also reveals the presence of a solvent-exposed redox-sensitive disulphide bridge, unique among the subtilisin family, that likely acts as a regulator of protease activity in the parasite.


  • Organizational Affiliation

    Division of Parasitology, MRC National Institute for Medical Research, Mill Hill, London NW7 1AA, UK.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Subtilisin-like serine protease344Plasmodium falciparumMutation(s): 0 
Gene Names: sub-1
EC: 3.4.21.61
UniProt
Find proteins for O61142 (Plasmodium falciparum)
Explore O61142 
Go to UniProtKB:  O61142
Entity Groups  
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UniProt GroupO61142
Sequence Annotations
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
NIMP.M7 Fab light chain212Mus musculusMutation(s): 0 
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  • Reference Sequence
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
NIMP.M7 Fab heavy chain220Mus musculusMutation(s): 0 
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  • Reference Sequence
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
Subtilisin-like serine proteaseD [auth P]93Plasmodium falciparumMutation(s): 0 
Gene Names: sub-1
EC: 3.4.21.61
UniProt
Find proteins for O61142 (Plasmodium falciparum)
Explore O61142 
Go to UniProtKB:  O61142
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO61142
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.25 Å
  • R-Value Free: 0.237 
  • R-Value Work: 0.195 
  • R-Value Observed: 0.198 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 73.5α = 90
b = 74.79β = 103.33
c = 78.85γ = 90
Software Package:
Software NamePurpose
XDSdata scaling
PHENIXmodel building
PHENIXrefinement
XDSdata reduction
SCALEPACKdata scaling
PHENIXphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2014-05-07
    Type: Initial release
  • Version 1.1: 2014-06-11
    Changes: Database references
  • Version 1.2: 2023-09-20
    Changes: Data collection, Database references, Derived calculations, Refinement description