4tu3

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Crystal structure of yeast Sac1/Vps74 complexCrystal structure of yeast Sac1/Vps74 complex

Structural highlights

4tu3 is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, RCSB, PDBsum

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[1]

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

References

  1. Cai Y, Deng Y, Horenkamp F, Reinisch KM, Burd CG. Sac1-Vps74 structure reveals a mechanism to terminate phosphoinositide signaling in the Golgi apparatus. J Cell Biol. 2014 Aug 18;206(4):485-91. doi: 10.1083/jcb.201404041. Epub 2014 Aug, 11. PMID:25113029 doi:http://dx.doi.org/10.1083/jcb.201404041

4tu3, resolution 3.19Å

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