4ll8

Complex of carboxy terminal domain of Myo4p and She3p middle fragment

spinqualitylabelsall models 4ll8, resolution 3.58Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ll8 is a 3 chain structure with sequence from Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.578Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MYO4_YEAST Part of the mRNA localization machinery that restricts accumulation of certain proteins to the bud and in the daughter cell. Recruited to specific mRNAs including the ASH1 mRNA, coding for a repressor of the HO endonuclease, via its interaction with SHE3. Publication Abstract from PubMed Myosin 4 protein (Myo4p), one of five distinct myosins of yeast, is dedicated to cytoplasmic transport of two types of cargos, zipcoded messenger ribonucleoprotein particles (mRNPs) and tubular endoplasmic reticulum (tER). Neither cargo binds directly to Myo4p. Instead, swi5p-dependent HO expression 3 protein (She3p) serves as an "adaptor" that contains three binding modules, one for Myo4p and one each for zipcoded mRNP and tER. The assembly of a transport-competent motor complex is poorly understood. Here, we report that Myo4p*She3p forms a stable 1:2 heterotrimer in solution. In the Myo4p*She3p crystal structure, Myo4p's C-terminal domain (CTD) assumes a lobster claw-shaped form, the minor prong of which adheres to a pseudocoiled-coil region of She3p. The extensive Myo4p*She3p interactome buries 3,812 A(2) surface area and is primarily hydrophobic. Because the Myo4p*She3p heterotrimer contains only one myosin molecule, it is not transport-competent. By stepwise reconstitution, we found a single molecule of synthetic oligonucleotide (representing the mRNA zipcode element) bound to a single tetramer of zipcode binding protein She2p to be sufficient for Myo4p*She3p dimerization. Therefore, cargo initiates cross-linking of two Myo4p*She3p heterotrimers to an ensemble that contains two myosin molecules obligatory for movement. An additional crystal structure comprising an overlapping upstream portion of She3p showed continuation of the pseudocoiled-coil structure and revealed another highly conserved surface region. We suggest this region as a candidate binding site for a yet unidentified tER ligand. We propose a model whereby zipcoded mRNP and/or tER ligands couple two Myo4p*She3p heterotrimers and thereby generate a transport-competent motor complex either for separate transport or cotransport of these two cargos. Structure of a myosin*adaptor complex and pairing by cargo.,Shi H, Singh N, Esselborn F, Blobel G Proc Natl Acad Sci U S A. 2014 Mar 25;111(12):E1082-90. doi:, 10.1073/pnas.1401428111. Epub 2014 Feb 12. PMID:24522109 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Myosin 3D Structures

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