4AV8

Kluyveromyces lactis Hsv2 complete loop 6CD

Summary for 4AV8

• Entry DOI: 10.2210/pdb4av8/pdb
• Descriptor: SVP1-LIKE PROTEIN 2 (1 entity in total)
• Functional Keywords: lipid binding protein
• Biological source: KLUYVEROMYCES LACTIS
• Cellular location: Vacuole membrane; Peripheral membrane protein (By similarity): Q6CN23
• Total number of polymer chains: 1
• Total formula weight: 39219.94

Authors

Krick, R.,Busse, R.A.,Scacioc, A.,Stephan, M.,Janshoff, A.,Thumm, M.,Kuhnel, K. (deposition date: 2012-05-24, release date: 2012-06-13, Last modification date: 2023-12-20)

Primary citation

Krick, R.,Busse, R.A.,Scacioc, A.,Stephan, M.,Janshoff, A.,Thumm, M.,Kuhnel, K.
Structural and Functional Characterization of the Two Phosphoinositide Binding Sites of Proppins, a Beta-Propeller Protein Family.
Proc.Natl.Acad.Sci.USA, 109:E2042-, 2012

PubMed Abstract: β-propellers that bind polyphosphoinositides (PROPPINs), a eukaryotic WD-40 motif-containing protein family, bind via their predicted β-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-Å 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 β-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.

PubMed: 22753491
DOI: 10.1073/PNAS.1205128109

Experimental method

X-RAY DIFFRACTION (3.35 Å)