3dm0 | pdb_00003dm0
Maltose Binding Protein fusion with RACK1 from A. thaliana
Structural highlights
FunctionMALE_ECOLI Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.GBLPA_ARATH Major component of the RACK1 regulatory proteins that play a role in multiple signal transduction pathways. Involved in multiple hormone responses and developmental processes (PubMed:16829549, PubMed:18715992, PubMed:18947417). MAPK cascade scaffolding protein involved in the protease IV and ArgC signaling pathway but not the flg22 pathway (PubMed:25731164).[1] [2] [3] [4] 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 receptor for activated C-kinase 1 (RACK1) is a highly conserved WD40 repeat scaffold protein found in a wide range of eukaryotic species from Chlamydymonas to plants and humans. In tissues of higher mammals, RACK1 is ubiquitously expressed and has been implicated in diverse signaling pathways involving neuropathology, cellular stress, protein translation, and developmental processes. RACK1 has established itself as a scaffold protein through physical interaction with a myriad of signaling proteins ranging from kinases, phosphatases, ion channels, membrane receptors, G proteins, IP3 receptor, and with widely conserved structural proteins associated with the ribosome. In the plant Arabidopsis thaliana, RACK1A is implicated in diverse developmental and environmental stress pathways. Despite the functional conservation of RACK1-mediated protein-protein interaction-regulated signaling modes, the structural basis of such interactions is largely unknown. Here we present the first crystal structure of a RACK1 protein, RACK1 isoform A from Arabidopsis thaliana, at 2.4 A resolution, as a C-terminal fusion of the maltose binding protein. The structure implicates highly conserved surface residues that could play critical roles in protein-protein interactions and reveals the surface location of proposed post-transcriptionally modified residues. The availability of this structure provides a structural basis for dissecting RACK1-mediated cellular signaling mechanisms in both plants and animals. Structure of a signal transduction regulator, RACK1, from Arabidopsis thaliana.,Ullah H, Scappini EL, Moon AF, Williams LV, Armstrong DL, Pedersen LC Protein Sci. 2008 Oct;17(10):1771-80. Epub 2008 Aug 20. PMID:18715992[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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