View source for 4av8


==Kluyveromyces lactis Hsv2 complete loop 6CD==
<StructureSection load='4av8' size='340' side='right'caption='[[4av8]], [[Resolution|resolution]] 3.35&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4av8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Kluyveromyces_lactis Kluyveromyces lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AV8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AV8 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.35&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4av8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4av8 OCA], [https://pdbe.org/4av8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4av8 RCSB], [https://www.ebi.ac.uk/pdbsum/4av8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4av8 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HSV2_KLULA HSV2_KLULA] Involved in mitochondrial or peroxisomal functions and amino acid signaling pathways (By similarity).
<div style="background-color:#fffaf0;">
== 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<ref>PMID:22753491</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4av8" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Kluyveromyces lactis]]
[[Category: Large Structures]]
[[Category: Busse RA]]
[[Category: Janshoff A]]
[[Category: Krick R]]
[[Category: Kuhnel K]]
[[Category: Scacioc A]]
[[Category: Stephan M]]
[[Category: Thumm M]]