4tu3: Difference between revisions
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''' | ==Crystal structure of yeast Sac1/Vps74 complex== | ||
<StructureSection load='4tu3' size='340' side='right' caption='[[4tu3]], [[Resolution|resolution]] 3.19Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4tu3]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TU3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TU3 FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4tu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tu3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4tu3 RCSB], [http://www.ebi.ac.uk/pdbsum/4tu3 PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Sac1 is a phosphoinositide phosphatase of the endoplasmic reticulum and Golgi apparatus that controls organelle membrane composition principally via regulation of phosphatidylinositol 4-phosphate signaling. We present a characterization of the structure of the N-terminal portion of yeast Sac1, containing the conserved Sac1 homology domain, in complex with Vps74, a phosphatidylinositol 4-kinase effector and the orthologue of human GOLPH3. The interface involves the N-terminal subdomain of the Sac1 homology domain, within which mutations in the related Sac3/Fig4 phosphatase have been linked to Charcot-Marie-Tooth disorder CMT4J and amyotrophic lateral sclerosis. Disruption of the Sac1-Vps74 interface results in a broader distribution of phosphatidylinositol 4-phosphate within the Golgi apparatus and failure to maintain residence of a medial Golgi mannosyltransferase. The analysis prompts a revision of the membrane-docking mechanism for GOLPH3 family proteins and reveals how an effector of phosphoinositide signaling serves a dual function in signal termination. | |||
Sac1-Vps74 structure reveals a mechanism to terminate phosphoinositide signaling in the Golgi apparatus.,Cai Y, Deng Y, Horenkamp F, Reinisch KM, Burd CG J Cell Biol. 2014 Aug 18;206(4):485-91. doi: 10.1083/jcb.201404041. Epub 2014 Aug, 11. PMID:25113029<ref>PMID:25113029</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Cai, Y.]] | |||
[[Category: Horenkamp, F A.]] | |||
[[Category: Reinisch, K R.]] | |||
[[Category: Golgi apparatus]] | |||
[[Category: Phosphatidylinositol phosphate]] | |||
[[Category: Phosphoric monoester hydrolase]] | |||
[[Category: Protein complex]] | |||
Revision as of 08:44, 27 August 2014
Crystal structure of yeast Sac1/Vps74 complex
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