3lku | pdb_00003lku
Crystal structure of S. cerevisiae Get4 in complex with an N-terminal fragment of Get5
Structural highlights
Function[YO164_YEAST] May play a role in insertion of tail-anchored proteins into the endoplasmic reticulum membrane.[1] [MDY2_YEAST] Required for efficient mating. Involved in the production of alpha-factor, the KAR9 and TUB1 location to the shmoo tip and nuclear migration into pheromone-induced shmoos.[2] [3] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe recently elucidated Get proteins are responsible for the targeted delivery of the majority of tail-anchored (TA) proteins to the endoplasmic reticulum. Get4 and Get5 have been identified in the early steps of the pathway mediating TA substrate delivery to the cytoplasmic targeting factor Get3. Here we report a crystal structure of Get4 and an N-terminal fragment of Get5 from Saccharomyces cerevisae. We show Get4 and Get5 (Get4/5) form an intimate complex that exists as a dimer (two copies of Get4/5) mediated by the C-terminus of Get5. We further demonstrate that Get3 specifically binds to a conserved surface on Get4 in a nucleotide dependent manner. This work provides further evidence for a model in which Get4/5 operates upstream of Get3 and mediates the specific delivery of a TA substrate. Structural characterization of the Get4/Get5 complex and its interaction with Get3.,Chartron JW, Suloway CJ, Zaslaver M, Clemons WM Jr Proc Natl Acad Sci U S A. 2010 Jul 6;107(27):12127-32. Epub 2010 Jun 16. PMID:20554915[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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