2X43

STRUCTURAL BASIS OF MOLECULAR RECOGNITION BY SHERP AT MEMBRANE SURFACES


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 10 
  • Conformers Submitted: 10 
  • Selection Criteria: LEAST VIOLATIONS 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Structural Basis of Moelcular Recognition by the Leishmania Small Hydrophilic Endoplasmic Reticulum-Associated Protein, Sherp, at Membrane Surfaces

Moore, B.Miles, A.J.Guerra, C.G.Simpson, P.Iwata, M.Wallace, B.A.Matthews, S.J.Smith, D.F.Brown, K.A.

(2011) J Biol Chem 286: 9246

  • DOI: https://doi.org/10.1074/jbc.M110.130427
  • Primary Citation of Related Structures:  
    2X43

  • PubMed Abstract: 

    The 57-residue small hydrophilic endoplasmic reticulum-associated protein (SHERP) shows highly specific, stage-regulated expression in the non-replicative vector-transmitted stages of the kinetoplastid parasite, Leishmania major, the causative agent of human cutaneous leishmaniasis. Previous studies have demonstrated that SHERP localizes as a peripheral membrane protein on the cytosolic face of the endoplasmic reticulum and on outer mitochondrial membranes, whereas its high copy number suggests a critical function in vivo. However, the absence of defined domains or identifiable orthologues, together with lack of a clear phenotype in transgenic parasites lacking SHERP, has limited functional understanding of this protein. Here, we use a combination of biophysical and biochemical methods to demonstrate that SHERP can be induced to adopt a globular fold in the presence of anionic lipids or SDS. Cross-linking and binding studies suggest that SHERP has the potential to form a complex with the vacuolar type H(+)-ATPase. Taken together, these results suggest that SHERP may function in modulating cellular processes related to membrane organization and/or acidification during vector transmission of infective Leishmania.


  • Organizational Affiliation

    Division of Cell and Molecular Biology, Centre for Molecular Microbiology and Infection, Imperial College London, Exhibition Road, London SW7 2AZ, United Kingdom.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
SHERPA [auth S]67Leishmania majorMutation(s): 0 
UniProt
Find proteins for Q9XTN3 (Leishmania major)
Explore Q9XTN3 
Go to UniProtKB:  Q9XTN3
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9XTN3
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 10 
  • Conformers Submitted: 10 
  • Selection Criteria: LEAST VIOLATIONS 

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2010-11-24
    Type: Initial release
  • Version 1.1: 2017-04-19
    Changes: Other
  • Version 1.2: 2024-05-15
    Changes: Data collection, Database references, Other