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6iyy

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Revision as of 07:52, 10 April 2019

Crystal structure of human WIPI3,loop deletion mutant

Structural highlights

6iyy is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	WIPI3 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[WIPI3_HUMAN] The disease may be caused by mutations affecting the gene represented in this entry.

Function

[WIPI3_HUMAN] Component of the autophagy machinery that controls the major intracellular degradation process by which cytoplasmic materials are packaged into autophagosomes and delivered to lysosomes for degradation (PubMed:28561066). Binds phosphatidylinositol 3-phosphate (PtdIns3P) forming on membranes of the endoplasmic reticulum upon activation of the upstream ULK1 and PI3 kinases and is recruited at phagophore assembly sites where it regulates the elongation of nascent phagophores downstream of WIPI2 (PubMed:28561066). In the cellular response to starvation, may also function together with the TSC1-TSC2 complex and RB1CC1 in the inhibition of the mTORC1 signaling pathway (PubMed:28503735).^[1] ^[2]

Publication Abstract from PubMed

WIPI proteins are mammalian PROPPIN family members that bind to phosphoinositides and play prominent roles in autophagosome biogenesis. Two phosphoinositide-binding sites were previously described in yeast PROPPIN Hsv2 but remain to be determined in mammalian WIPI proteins. Here, we characterized four human WIPI proteins (WIPI1-4) and solved the structure of WIPI3. WIPI proteins can bind to PI(3)P and PI(3,5)P2 and adopt a conventional seven-bladed beta-propeller fold. The structure of WIPI3 revealed that WIPI proteins also contain two sites embedded in blades 5 and 6 for recognizing phosphoinositides, resembling that in Hsv2. Structural comparison further demonstrated that the two conserved phosphoinositide-binding sites in PROPPIN proteins are not identical but intrinsically tend to recognize different types of phosphoinositides. This work provides the structural evidence to support the conservation of the two phosphoinositide-binding sites in WIPI proteins and also uncovers the potential phosphoinositide-binding selectivity for each site.

Structural Conservation of the Two Phosphoinositide-Binding Sites in WIPI Proteins.,Liang R, Ren J, Zhang Y, Feng W J Mol Biol. 2019 Feb 22. pii: S0022-2836(19)30096-8. doi:, 10.1016/j.jmb.2019.02.019. PMID:30797857^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Suleiman J, Allingham-Hawkins D, Hashem M, Shamseldin HE, Alkuraya FS, El-Hattab AW. WDR45B-related intellectual disability, spastic quadriplegia, epilepsy, and cerebral hypoplasia: A consistent neurodevelopmental syndrome. Clin Genet. 2018 Feb;93(2):360-364. doi: 10.1111/cge.13054. Epub 2017 Sep 7. PMID:28503735 doi:http://dx.doi.org/10.1111/cge.13054
↑ Bakula D, Muller AJ, Zuleger T, Takacs Z, Franz-Wachtel M, Thost AK, Brigger D, Tschan MP, Frickey T, Robenek H, Macek B, Proikas-Cezanne T. WIPI3 and WIPI4 beta-propellers are scaffolds for LKB1-AMPK-TSC signalling circuits in the control of autophagy. Nat Commun. 2017 May 31;8:15637. doi: 10.1038/ncomms15637. PMID:28561066 doi:http://dx.doi.org/10.1038/ncomms15637
↑ Liang R, Ren J, Zhang Y, Feng W. Structural Conservation of the Two Phosphoinositide-Binding Sites in WIPI Proteins. J Mol Biol. 2019 Feb 22. pii: S0022-2836(19)30096-8. doi:, 10.1016/j.jmb.2019.02.019. PMID:30797857 doi:http://dx.doi.org/10.1016/j.jmb.2019.02.019

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6iyy"

@@ Line 3: / Line 3: @@
 <StructureSection load='6iyy' size='340' side='right'caption='[[6iyy]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6iyy]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IYY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6IYY FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6iyy]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IYY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6IYY FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">WIPI3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6iyy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6iyy OCA], [http://pdbe.org/6iyy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6iyy RCSB], [http://www.ebi.ac.uk/pdbsum/6iyy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6iyy ProSAT]</span></td></tr>
 </table>
@@ Line 24: / Line 25: @@
 __TOC__
 </StructureSection>
+[[Category: Human]]
 [[Category: Large Structures]]
 [[Category: Feng, W]]

6iyy

From Proteopedia

Revision as of 07:52, 10 April 2019

Crystal structure of human WIPI3,loop deletion mutant

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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