4tu3
From Proteopedia
(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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