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PDBsum entry 5dfz
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Contents |
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343 a.a.
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783 a.a.
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1224 a.a.
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113 a.a.
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341 a.a.
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49 a.a.
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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 and flexibility of the endosomal vps34 complex reveals the basis of its function on membranes.
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Authors
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K.Rostislavleva,
N.Soler,
Y.Ohashi,
L.Zhang,
E.Pardon,
J.E.Burke,
G.R.Masson,
C.Johnson,
J.Steyaert,
N.T.Ktistakis,
R.L.Williams.
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Ref.
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Science, 2015,
350,
aac7365.
[DOI no: ]
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PubMed id
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Abstract
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Phosphatidylinositol 3-kinase Vps34 complexes regulate intracellular membrane
trafficking in endocytic sorting, cytokinesis, and autophagy. We present the 4.4
angstrom crystal structure of the 385-kilodalton endosomal complex II
(PIK3C3-CII), consisting of Vps34, Vps15 (p150), Vps30/Atg6 (Beclin 1), and
Vps38 (UVRAG). The subunits form a Y-shaped complex, centered on the Vps34 C2
domain. Vps34 and Vps15 intertwine in one arm, where the Vps15 kinase domain
engages the Vps34 activation loop to regulate its activity. Vps30 and Vps38 form
the other arm that brackets the Vps15/Vps34 heterodimer, suggesting a path for
complex assembly. We used hydrogen-deuterium exchange mass spectrometry (HDX-MS)
to reveal conformational changes accompanying membrane binding and identify a
Vps30 loop that is critical for the ability of complex II to phosphorylate giant
liposomes on which complex I is inactive.
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