View source for 4v16


==KlHsv2 with loop 6CD replaced by a Gly-Ser linker==
<StructureSection load='4v16' size='340' side='right'caption='[[4v16]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4v16]] 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=4V16 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V16 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]] 2.8&#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=4v16 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v16 OCA], [https://pdbe.org/4v16 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v16 RCSB], [https://www.ebi.ac.uk/pdbsum/4v16 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v16 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 ==
PROPPINs (beta-propellers that bind polyphosphoinositides) are a family of PtdIns3P- and PtdIns(3,5)P2-binding proteins that play an important role in autophagy. We analyzed PROPPIN-membrane binding through isothermal titration calorimetry (ITC), stopped-flow measurements, mutagenesis studies, and molecular dynamics (MD) simulations. ITC measurements showed that the yeast PROPPIN family members Atg18, Atg21, and Hsv2 bind PtdIns3P and PtdIns(3,5)P2 with high affinities in the nanomolar to low-micromolar range and have two phosphoinositide (PIP)-binding sites. Single PIP-binding site mutants have a 15- to 30-fold reduced affinity, which explains the requirement of two PIP-binding sites in PROPPINs. Hsv2 bound small unilamellar vesicles with a higher affinity than it bound large unilamellar vesicles in stopped-flow measurements. Thus, we conclude that PROPPIN membrane binding is curvature dependent. MD simulations revealed that loop 6CD is an anchor for membrane binding, as it is the region of the protein that inserts most deeply into the lipid bilayer. Mutagenesis studies showed that both hydrophobic and electrostatic interactions are required for membrane insertion of loop 6CD. We propose a model for PROPPIN-membrane binding in which PROPPINs are initially targeted to membranes through nonspecific electrostatic interactions and are then retained at the membrane through PIP binding.

Characterization of PROPPIN-Phosphoinositide Binding and Role of Loop 6CD in PROPPIN-Membrane Binding.,Busse RA, Scacioc A, Krick R, Perez-Lara A, Thumm M, Kuhnel K Biophys J. 2015 May 5;108(9):2223-34. doi: 10.1016/j.bpj.2015.03.045. PMID:25954880<ref>PMID:25954880</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4v16" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Kluyveromyces lactis]]
[[Category: Large Structures]]
[[Category: Busse RA]]
[[Category: Krick R]]
[[Category: Kuhnel K]]
[[Category: Perez-Lara A]]
[[Category: Scacioc A]]
[[Category: Thumm M]]