4wnl

The X-ray structure of a RNA-binding protein complex

spinqualitylabelsall models 4wnl, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4wnl is a 8 chain structure with sequence from Saccharomyces cerevisiae AWRI1631 and 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 2.8Å Ligands: GOL, IPA, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SHE2_YEAST RNA-binding protein that binds specific mRNAs including the ASH1 mRNA, coding for a repressor of the HO endonuclease. Part of the mRNA localization machinery that restricts accumulation of certain proteins to the bud and in the daughter cell. Recruits the MYO4-SHE3 complex to the ASH1 mRNA. Recruites also LOC1 and PUF6 to ASH1 mRNA, which are required for translational repression of this mRNA. Publication Abstract from PubMed The segregation of approximately two dozen distinct mRNAs from yeast mother to daughter cell cytoplasm is a classical paradigm for eukaryotic mRNA transport. The information for transport resides in an mRNA element 40-100 nt in length, known as "zipcode." Targeted transport requires properly positioned actin filaments and cooperative loading of mRNA cargo to myosin. Cargo loading to myosin uses myosin 4 protein (Myo4p), swi5p-dependent HO expression 2 protein (She2p) and 3 protein (She3p), and zipcode. We previously determined a crystal structure of Myo4p and She3p, their 1:2 stoichiometry and interactome; we furthermore showed that the motor complex assembly requires two Myo4pShe3p heterotrimers, one She2p tetramer, and at least a single zipcode to yield a stable complex of [Myo4pShe3pShe2pzipcode] in 2:4:4:1 stoichiometry in vitro. Here, we report a structure at 2.8-A resolution of a cocrystal of a She2p tetramer bound to a segment of She3p. In this crystal structure, the She3p segment forms a striking hook that binds to a shallow hydrophobic pocket on the surface of each She2p subunit of the tetramer. Both She3p hook and cognate She2p binding pocket are composed of highly conserved residues. We also discovered a highly conserved region of She3p upstream of its hook region. Because this region consists of basic and aromatic residues, it likely represents part of She3p's binding activity for zipcode. Because She2p also exhibits zipcode-binding activity, we suggest that "hooking" She3p onto She2p aligns each of their zipcode-binding activities into a high-affinity site, thereby linking motor assembly to zipcode. Hooking She3p onto She2p for myosin-mediated cytoplasmic mRNA transport.,Singh N, Blobel G, Shi H Proc Natl Acad Sci U S A. 2015 Jan 6;112(1):142-7. doi: 10.1073/pnas.1423194112. , Epub 2014 Dec 22. PMID:25535369 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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