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2X43

STRUCTURAL BASIS OF MOLECULAR RECOGNITION BY SHERP AT MEMBRANE SURFACES

Summary for 2X43
Entry DOI10.2210/pdb2x43/pdb
DescriptorSHERP (1 entity in total)
Functional Keywordsmembrane protein
Biological sourceLEISHMANIA MAJOR
Total number of polymer chains1
Total formula weight7267.88
Authors
Moore, B.,Miles, A.J.,Guerra, C.G.,Simpson, P.,Iwata, M.,Wallace, B.A.,Matthews, S.J.,Smith, D.F.,Brown, K.A. (deposition date: 2010-02-09, release date: 2010-11-24, Last modification date: 2024-05-15)
Primary citationMoore, B.,Miles, A.J.,Guerra, C.G.,Simpson, P.,Iwata, M.,Wallace, B.A.,Matthews, S.J.,Smith, D.F.,Brown, K.A.
Structural Basis of Moelcular Recognition by the Leishmania Small Hydrophilic Endoplasmic Reticulum-Associated Protein, Sherp, at Membrane Surfaces
J.Biol.Chem., 286:9246-, 2011
Cited by
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.
PubMed: 21106528
DOI: 10.1074/JBC.M110.130427
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

226707

數據於2024-10-30公開中

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