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PDBsum entry 4yhc
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Structural protein
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PDB id
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4yhc
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References listed in PDB file
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Key reference
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Title
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Structure of the wd40 domain of scap from fission yeast reveals the molecular basis for srebp recognition.
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Authors
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X.Gong,
J.Li,
W.Shao,
J.Wu,
H.Qian,
R.Ren,
P.Espenshade,
N.Yan.
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Ref.
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Cell Res, 2015,
25,
401-411.
[DOI no: ]
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PubMed id
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Abstract
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The sterol regulatory element-binding protein (SREBP) and SREBP
cleavage-activating protein (SCAP) are central players in the SREBP pathway,
which control the cellular lipid homeostasis. SCAP binds to SREBP through their
carboxyl (C) domains and escorts SREBP from the endoplasmic reticulum to the
Golgi upon sterol depletion. A conserved pathway, with the homologues of SREBP
and SCAP being Sre1 and Scp1, was identified in fission yeast
Schizosaccharomyces pombe. Here we report the in vitro reconstitution of the
complex between the C domains of Sre1 and Scp1 as well as the crystal structure
of the WD40 domain of Scp1 at 2.1 Å resolution. The structure reveals an
eight-bladed β-propeller that exhibits several distinctive features from a
canonical WD40 repeat domain. Structural and biochemical characterization led to
the identification of two Scp1 elements that are involved in Sre1 recognition,
an Arg/Lys-enriched surface patch on the top face of the WD40 propeller and a
30-residue C-terminal tail. The structural and biochemical findings were
corroborated by in vivo examinations. These studies serve as a framework for the
mechanistic understanding and further functional characterization of the SREBP
and SCAP proteins in fission yeast and higher organisms.
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