5dfz | pdb_00005dfz

Structure of Vps34 complex II from S. cerevisiae.

spinqualitylabelsall models 5dfz, resolution 4.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5dfz is a 6 chain structure with sequence from Lama glama, Saccharomyces cerevisiae and Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function VPS38_YEAST Involved in endosome-to-Golgi retrograde transport as part of the VPS34 PI3-kinase complex II. This complex is required for the endosome-to-Golgi retrieval of PEP1 and KEX2, and the recruitment of VPS5 and VPS7, two components of the retromer complex, to endosomal membranes (probably through generating a specific pool of phosphatidylinositol 3-phosphate allowing the recruitment of the retromer complex proteins to the endosome). Mediates the interaction between VPS30 and the VPS34-VPS15 core complex, leading to the recruitment of VPS30 to the membrane. Publication Abstract from PubMed 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. Structure and flexibility of the endosomal Vps34 complex reveals the basis of its function on membranes.,Rostislavleva K, Soler N, Ohashi Y, Zhang L, Pardon E, Burke JE, Masson GR, Johnson C, Steyaert J, Ktistakis NT, Williams RL Science. 2015 Oct 9;350(6257):aac7365. doi: 10.1126/science.aac7365. PMID:26450213 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Serine/threonine protein kinase 3D structures Vacuolar protein sorting-associated protein 3D structures

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