2v52

Structure of MAL-RPEL2 complexed to G-actin

spinqualitylabelsall models 2v52, resolution 1.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2v52 is a 2 chain structure with sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ATP, GOL, LAB, MG Related: 1lcu, 2a42, 2aso, 1ijj, 1wua, 1o18, 1m8q, 1o1a, 1rfq, 1uy5, 1ma9, 2d1k, 1rdw, 1o1b, 1o1d, 2a40, 2a5x, 1qz5, 1nwk, 1j6z, 1sqk, 1atn, 1s22, 1t44, 2ff3, 1eqy, 1mvw, 2ff6, 2fxu, 1o1f, 1kxp, 2asp, 1rgi, 1o19, 1y64, 1alm, 1o1e, 1esv, 1p8z, 1h1v, 1o1c, 2vcp, 1o1g, 2a3z, 1lot, 2asm, 2a41, 2vyp, 1qz6, 2v51 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ACTS_RABIT] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. [MKL1_MOUSE] Transcriptional coactivator of serum response factor (SRF) with the potential to modulate SRF target genes. Suppresses TNF-induced cell death by inhibiting activation of caspases; its transcriptional activity is indispensable for the antiapoptotic function. It may up-regulate antiapoptotic molecules, which in turn inhibit caspase activation. Publication Abstract from PubMed Serum response factor transcriptional activity is controlled through interactions with regulatory cofactors such as the coactivator MAL/MRTF-A (myocardin-related transcription factor A). MAL is itself regulated in vivo by changes in cellular actin dynamics, which alter its interaction with G-actin. The G-actin-sensing mechanism of MAL/MRTF-A resides in its N-terminal domain, which consists of three tandem RPEL repeats. We describe the first molecular insights into RPEL function obtained from structures of two independent RPEL(MAL) peptide:G-actin complexes. Both RPEL peptides bind to the G-actin hydrophobic cleft and to subdomain 3. These RPEL(MAL):G-actin structures explain the sequence conservation defining the RPEL motif, including the invariant arginine. Characterisation of the RPEL(MAL):G-actin interaction by fluorescence anisotropy and cell reporter-based assays validates the significance of actin-binding residues for proper MAL localisation and regulation in vivo. We identify important differences in G-actin engagement between the two RPEL(MAL) structures. Comparison with other actin-binding proteins reveals an unexpected similarity to the vitamin-D-binding protein, extending the G-actin-binding protein repertoire. Molecular basis for G-actin binding to RPEL motifs from the serum response factor coactivator MAL.,Mouilleron S, Guettler S, Langer CA, Treisman R, McDonald NQ EMBO J. 2008 Nov 13. PMID:19008859 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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