4av9

Kluyveromyces lactis Hsv2

spinqualitylabelsall models 4av9, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4av9 is a 1 chain structure with sequence from Atcc 56498. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SO4 Related: 4av8 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [HSV2_KLULA] Involved in mitochondrial or peroxisomal functions and amino acid signaling pathways (By similarity). Publication Abstract from PubMed beta-propellers that bind polyphosphoinositides (PROPPINs), a eukaryotic WD-40 motif-containing protein family, bind via their predicted beta-propeller fold the polyphosphoinositides PtdIns3P and PtdIns(3,5)P(2) using a conserved FRRG motif. PROPPINs play a key role in macroautophagy in addition to other functions. We present the 3.0-A crystal structure of Kluyveromyces lactis Hsv2, which shares significant sequence homologies with its three Saccharomyces cerevisiae homologs Atg18, Atg21, and Hsv2. It adopts a seven-bladed beta-propeller fold with a rare nonvelcro propeller closure. Remarkably, in the crystal structure, the two arginines of the FRRG motif are part of two distinct basic pockets formed by a set of highly conserved residues. In comprehensive in vivo and in vitro studies of ScAtg18 and ScHsv2, we define within the two pockets a set of conserved residues essential for normal membrane association, phosphoinositide binding, and biological activities. Our experiments show that PROPPINs contain two individual phosphoinositide binding sites. Based on docking studies, we propose a model for phosphoinositide binding of PROPPINs. Structural and functional characterization of the two phosphoinositide binding sites of PROPPINs, a beta-propeller protein family.,Krick R, Busse RA, Scacioc A, Stephan M, Janshoff A, Thumm M, Kuhnel K Proc Natl Acad Sci U S A. 2012 Jul 2. PMID:22753491 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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