4tu3: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4tu3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4TU3 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4tu3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4TU3 FirstGlance]. <br> | ||
</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=4tu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tu3 OCA], [https://pdbe.org/4tu3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tu3 RCSB], [https://www.ebi.ac.uk/pdbsum/4tu3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tu3 ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.187Å</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=4tu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tu3 OCA], [https://pdbe.org/4tu3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tu3 RCSB], [https://www.ebi.ac.uk/pdbsum/4tu3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tu3 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
Latest revision as of 10:23, 27 September 2023
Crystal structure of yeast Sac1/Vps74 complexCrystal structure of yeast Sac1/Vps74 complex
Structural highlights
FunctionSAC1_YEAST Phosphoinositide phosphatase that hydrolyzes PtdIns(3)P and PtdIns(4)P. Has low activity towards PtdIns(3,5)P2. May be involved in the coordination of the activities of the secretory pathway and the actin cytoskeleton.[1] [2] Publication Abstract from PubMedSac1 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[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also
References
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